AMYB_SOYBN.struc:
7777485|Sweet potato beta-amylase is a tetramer of identical subunits, which are arranged to exhibit 222 molecular symmetry. 
7777485|Its subunit consists of 498 amino acid residues (Mr 55,880).
7777485|The refined subunit model contains 3,863 nonhydrogen protein atoms (488 amino acid residues) and 319 water oxygen atoms.
7777485|The subunit structure of sweet potato beta-amylase (crystallized in the absence of alpha-cyclodextrin) is very similar to that of soybean beta-amylase (complexed with alpha-cyclodextrin).
7777485|Each subunit of sweet potato beta-amylase is composed of a large (alpha/beta)8 core domain, a small one made up of three long loops [L3 (residues 91-150), L4 (residues 183-258), and L5 (residues 300-327)], and a long C-terminal loop formed by residues 445-493. 
7777485|Conserved Glu 187, believed to play an important role in catalysis, is located at the cleft between the (alpha/beta)8 barrel core and a small domain made up of three long loops (L3, L4, and L5). 
7777485|Conserved Cys 96, important in the inactivation of enzyme activity by sulfhydryl reagents, is located at the entrance of the (alpha/beta)8 barrel.
2430952|The major acidic peptide, Pep-4, was a heptapeptide with a molecular weight of 766. 
2430952|The N-terminal 9 amino acid sequence of soybean beta-amylase was deduced to be acetyl-Ala-Thr-Ser-Asp-Ser-Asn-Met-(Gly-Leu) from the results of sequence analysis of Pep-4 and amino acid analysis of other acidic peptides.
8103452|The complete amino acid sequence of a subunit of sweet potato beta-amylase, a homotetramer, was established by sequence analysis of peptides obtained by digestions with Achromobacter protease I and Staphylococcus aureus V8 protease and by cyanogen bromide cleavage of the S-carboxymethylated subunit. 
8103452|The subunit of the enzyme is a single polypeptide consisting of 498 amino acid residues. 
8103452|It showed 50-60% identity in the amino acid sequence with those of beta-amylases from soybean and barley, while it about 25% with those of three bacterial beta-amylases deduced from the cDNA sequences. 
8103452|Sequence analysis of the inactivated enzyme revealed that Glu187 was specifically esterified by the affinity labeling with the above reagent, proposing that Glu187 is a potent candidate involved directly in the catalysis with this plant beta-amylase.
9847126|The beta-amylase cDNA encoded a 55.95-kD polypeptide with a deduced amino acid sequence showing high similarity to other plant beta-amylases. 
1837016|Unlike beta-amylases from other origins, the sweet potato beta-amylase is a tetramer of identical subunits, and it also bears starch phosphorylase-inhibitor activity. 
1837016|The cDNA insert contained 1,494 base pairs of an open reading frame which codes for the 499-amino-acid-long precursor to the subunit of beta-amylase. 
1837016|An amino acid sequence identical to the N-terminal amino acid sequence of the mature subunit appeared immediately after the initiator methionine of the precursor, indicating that the subunit of beta-amylase is synthesized as a mature form. 
1837016|Comparison of the amino acid sequences of subunits of sweet potato beta-amylase and seed beta-amylases from barley and soybean indicated that these enzymes share about 68% amino acid identities among each other.
8334116|The model contains 491 amino acid residues, 319 water molecules, 1 sulfate ion, and 1 alpha-cyclodextrin molecule. 
8334116|The protein consists of a core with an (alpha/beta)8 supersecondary structure, plus a smaller globular region formed by long loops (L3, L4, and L5) extending from beta-strands beta 3, beta 4, and beta 5. 
8334116|Between the two regions is a cleft that opens into a pocket whose floor contains the postulated catalytic center near the carboxyl group of Glu 186. 
8334116|Rather, it occupies most of the cleft entrance, strongly suggesting that alpha-cyclodextrin inhibits catalysis by blocking substrate access to the more deeply located reaction center.
8334116|Of the various alpha-cyclodextrin interactions with protein residues in loops L4, L5, L6, and L7, most notable is the shallow inclusion complex formed with Leu 383 (in L7, on the core side of the cleft) through contacts of its methyl groups with the C-3 atoms of four of the ligand's D-glucopyranosyl residues. 
8334116|All six residues of the bound alpha-cyclodextrin are of 4C1 conformation and are joined by alpha-1,4 linkages with similar torsional angles to form a nearly symmetrical torus as reported for crystalline inclusion complexes with alpha-cyclodextrin. 
8334116|We envision a significant role for the methyl groups of Leu 383 at the cleft entrance with respect to the productive binding of the outer chains of starch.
8174545|To determine which amino acid residues are essential for the catalytic activity of soybean beta-amylase, deoxyoligonucleotide site-directed mutagenesis was employed against aspartyl, glutamyl, and cysteinyl residues located in highly conserved regions found in beta-amylase family to date. 
8174545|Both substitution of aspartic acid at position 101 and that of glutamic acid at position 186 of the enzyme by neutral and acidic amino acids, respectively, led to the complete elimination of activity, but did not induce any significant changes in circular dichroic spectra or the binding affinity for cyclomaltohexaose, a substrate analogue. 
8174545|Taking account of the results obtained here, the above two amino acid residues are involved in the catalytic site of soybean beta-amylase. 
8174545|The replacement of glutamic acid at position 345 decreased activity to below 6% of the non-mutant level, implying that this residue may also play a crucial role in beta-amylase activity, although it may not be involved at the catalytic site itself. 
8174545|In contrast, substitution of cysteinyl residue at position 95 by a serinyl residue led to a drastic reducing of the optimal temperature (from 50 degrees C to 30 degrees C), suggesting that this cysteinyl residue is responsible for the thermal stability of the enzyme.
8011643|Two molecules of beta-maltose substrate bind to the protein in tandem, with some maltotetraose enzymic condensation product sharing the same binding sites. 
8011643|The catalytic center, located between the bound disaccharides and found deeper in the pocket than where the inhibitor alpha-cyclodextrin binds, is characterized by the presence of oppositely disposed carboxyl groups of two conserved glutamic acid residues. 
8011643|The OE2 carboxyl of Glu 186 is below the plane of the penultimate glucose residue (Glc 2) of bound maltotetraose, 2.6 A from the oxygen atom of that ligand's penultimate alpha-1,4-glucosidic linkage. 
8011643|The OE2 carboxyl of Glu 380 lies above the plane of Glc 2, 2.8 A from the O-1 atom of the more deeply bound beta-maltose. 
8011643|Saccharide binding does not alter the spatial coordinates of these two carboxyl groups or the overall conformation of the 57-kDa protein. 
8011643|However, the saccharide complexes of the active enzyme are associated with a significant (10 A) local conformational change in a peptide segment of a loop (L3) that borders the active site pocket.
9046591|The cDNA encodes a predicted product of 488 amino acids with significant similarity to known beta-amylases from barley (Hordeum vulgare), rye (Secale cereale), and rice (Oryza sativa). 
9046591|Glycine-rich repeats found in the carboxyl terminus of the endosperm-specific beta-amylase of barley and rye are absent from the maize gene product. 
9046591|The N-terminal sequence of the first 20 amino acids of a beta-amylase peptide derived from purified protein is identical to the 5th through 24th amino acids of the predicted cDNA product, indicating the absence of a conventional signal peptide in the maize protein. 
8188635|The beta-amylase was deduced to be composed of 535 amino acid residues and its molecular weight was calculated to be 59,610. 
8188635|Kreis et al. reported that the beta-amylase cDNA from barley (cultivar Hiproly) was 1,754 bp in length and coded for a polypeptide of 535 amino acids [Eur. J. Biochem. (1987) 169, 517-525]. 
8188635|A comparison of the beta-amylase sequences from Haruna two-rows and Hiproly barleys revealed nine differences in the nucleotide sequence which resulted in three changes in the amino acid residues and 21 additional nucleotides at its 3'-end in the cultivar Haruna two-rows. 
8188635|Lundgard and Svensson pointed out that 23 amino acid residues of the peptide fragment derived from the COOH-terminal region of barley (cultivar Gula) beta-amylase were in agreement with the deduced amino acid sequence reported by Kreis et al., with the exception of a single position (Met-527 compared to Ile) [Carlsberg Res. Commun. (1986) 51, 487-491].
8188635|In the cases of beta-amylases from soybean and sweet potato, the positions that corresponded to those at 233 and 347 in the amino acid sequence of beta-amylase from barley were Ala and Ser, respectively.
8319688|The cDNA contained an open-reading frame composed of 496 amino acids. 
8319688|His93, involving an imidazole, and Asp348, involving a carboxylate, in the highly conserved regions within the beta-amylases were replaced by Arg (H93R) and Ash (D348N) by site-directed mutagenesis, respectively. 
2474529|A radioactive peptide was finally isolated and its amino acid sequence was determined to be 181Leu-Gly-Pro-Ala-Gly-Glu186. 
2474529|It was concluded that the carboxylate of Glu-186 is a functional group at the catalytic site of soybean beta-amylase.
1491009|Preliminary chain tracing showed that the enzyme folded into large and small domains. 
1491009|The large domain has a (beta alpha)8 super-secondary structure, while the smaller one is formed from two long loops extending from the beta 3 and beta 4 strands of the (beta alpha)8 structure. 
1491009|The interface of the two domains together with shorter loops from the (beta alpha)8 structure form a deep cleft, in which alpha-cyclodextrin binds slightly away from the center. 
ANXB_HUMAN.struc:
7508441|The longest open reading frame encodes a 505-amino acid polypeptide, with a predicted molecular mass of 54.4 kDa. 
7508441|cDNA sequencing revealed that the 56K cDNA shares a high degree of homology in both nucleotide (87%) and amino acid sequence (92.5%) with bovine annexin XI, indicating that the 56K cDNA encodes the human homologue of annexin XI, a member of the Ca(2+)-dependent phospholipid binding protein family. 
7508441|Patients' sera recognize preferentially the N-terminal region of the protein, which is specific for 56K/annexin XI and not shared by other annexins, indicating that the autoimmune response to 56K/annexin XI in these patients is specific for this annexin family member.
11013079|The 5' regions consist of untranslated exon 1, followed by an extensive intron 1 comprising almost half the total gene length of >40 kb, and additional GC-rich exons 2-5 encoding the proline- and glycine-rich amino-terminus.
1535225|Annexin XI isoforms are predicted to differ at the amino-terminus, suggesting that they may have distinct biological roles.
8938449|The open reading frame was flanked by long, untranslated regions and encoded a 503-amino-acid protein with 93.1% identity to its human orthologue. 
8938449|Its 189-aa amino terminus corresponded to the widely expressed variant 1 of two possible, alternatively spliced forms. 
8938449|A previously described peptide from Aplysia brasiliana was identified as a closely related invertebrate homologue. 
8938449|Since annexin XI is known to be localized in the nucleus at certain stages of development, the identification of a region in tetrad repeats 3 and 4 resembling the "chromo box" domain may be relevant to a nuclear regulatory function of annexin XI. 
1380798|CAP-50 cDNA encodes a 503 residue protein with a calculated M(r) of 54,043 and shows that the protein is composed of four imperfect repeats and hydrophobic N-terminal region. 
1380798|C-terminal region including four imperfect repeats shows 58.1% identity with human synexin (annexin VII), 48.0% identity with annexin I, 47.4% identity with annexin II, 60.1% identity with annexin IV, 54.5% identity with annexin V. 
1380798|Hydrophobic N-terminal region composed of 202 amino acid residues is not homologous with other annexin proteins suggesting that CAP-50 is a novel member of annexin family proteins.
1372001|Each protein consists of a conserved core domain having four (or eight) repeats of a segment approximately 70 amino acids in length and a nonconserved, usually short, amino-terminal domain. 
1372001|The 503-amino acid deduced protein consists of a core domain of four annexin repeats and a long amino-terminal domain rich in glycine, proline, and tyrosine. 
BRS3_HUMAN.struc:
8131855| The deduced amino acid sequence shows about 86% identity to that of guinea pig bombesin receptor.
9573346|This family of heptahelical, G-protein coupled receptors includes the gastrin-releasing peptide receptor (GRP-R, or bb2), neuromedin B receptor (NMB-R, or bb1), and the bombesin receptor subtype 3 (BRS-3, or bb3). 
1325907|The cloned cDNA encodes a 399-amino-acid protein and shows the highest amino acid similarity to members of the bombesin receptor family; 52% and 47% similarity to the gastrin-releasing-peptide (GRP) receptor and the neuromedin-B receptor, respectively. 
10425452|The predicted amino acid sequence of ovine BRS-3 has approximately 85% identity with the human, mouse and guinea pig receptors. 
10425452|Highly conserved amino acids important in mediating receptor G-protein coupling to second messengers and important in ligand binding were found to be conserved in ovine BRS-3. 
10425452|One potentially important deviation was noted: ovine BRS-3 possesses an arginine residue at position 294 instead of a histidine residue as found in all other BRS-3. 
10425452|His(294) was previously identified as important in ligand-receptor interactions while Arg(294) was implicated in high ligand affinity. 
9262170|Comparison of the mouse and human receptor sequences indicates 90% (NMB-R) and 85% (BRS-3) sequence homology at the amino-acid level. 
CB2R_HUMAN.struc:
7689702|Progress stemmed initially from the synthesis of potent derivatives of delta 9-THC, and more recently from the cloning of a gene encoding a G-protein-coupled receptor for cannabinoids. 
10688601|Furthermore, unlike the CB(1) receptor, the sequences of the mouse and human CB(2) receptor are divergent, raising the possibility of species specificity. 
10688601|Sequence analysis of the coding region of the rat CB(2) genomic clone indicates 90% nucleic acid identity (93% amino acid identity) between rat and mouse and 81% nucleic acid identity (81% amino acid identity) between rat and human. 
8679694|The 3.7 kb sequence contains an open reading frame encoding a protein of 347 residues sharing 82% overall identity with the only other known peripheral receptor, human CB2 (hCB2) and shorter than hCB2 by 13 amino acids at the carboxyl terminus. 
9261404|The Cnr2 gene encodes a seven-transmembrane G-protein-coupled receptor which is normally expressed in hematopoietic tissues. 
12084572|The rat peripheral cannabinoid receptor (rCB2) was cloned from a Sprague-Dawley rat spleen cDNA library and when translated, encodes a protein of 410 amino acids. 
9261404|Alignment of rCB2 with mouse (mCB2) and human (hCB2) peripheral cannabinoid receptors reveals a high degree of homology except in the carboxy terminus where rCB2 is 50 and 63 residues longer than hCB2 and mCB2, respectively. 
DVL3_MOUSE.struc:
8922524|The predicted amino acid sequence shares 64 and 62% identity to Dvl1 and Dvl2, respectively. 
8922524|The region of highest conservation between all three Dvl coding regions, at 97% identity, is noted at the PDZ domain (also termed the DHR domain or GLGF motif), a motif of 60 amino acids present in all dishevelled encoded proteins and first described in the Drosophila discs large (dlg) tumor suppressor gene.
8817329|We have isolated and characterized cDNA clones from two different human dsh-homologous genes, designated as DVL-1 and DVL-3.
8817329|DVL-1 and DVL-3 putative protein products show 64% amino acid identity.
8817329|The DVL-1 product is 50% identical to dsh and 92% to a murine dsh homologue (Dvl-1). 
8644734|The isolated cDNAs exhibit high amino acid homology with the mouse and Xenopus Dvl-1 gene, the only other vertebrate dsh homologues so far isolated.
8887313|The Dvl2 amino acid sequence is equally related to the dsh sequence as is that of Dvl1, but Dvl2 is most similar to the Xenopus homolog Xdsh.
8149913|The dishevelled gene encodes a novel intracellular protein that shares an amino acid motif with several other proteins that are found associated with cell junctions.
9192851|Three human genes encoding proteins homologous to Drosophila Dishevelled protein were cloned and characterized. 
9192851|Amino acid similarity between the different Dishevelled proteins is concentrated in three highly conserved regions. 
9192851|Two of these regions do not exhibit significant sequence similarity with other known proteins; the third is similar to the discs-large homology region, which was first found in a Drosophila Discs-large tumor suppressor protein (also known as GLGF or PDZ domain).
9298901|Mice completely deficient for Dvl1, one of three mouse homologs of the Drosophila segment polarity gene Dishevelled, were created by gene targeting. 
8288125|The Drosophila Wnt-1 homolog, wingless (wg), is involved in the signaling of patterning information in several contexts. 
8288125|dsh is expressed uniformly in the embryo and encodes a novel protein with no known catalytic motifs, although it shares a domain of homology with several junction-associated proteins. 
9344861|A human homologue of Dsh (DVL-1) has recently been described. 
9344861|Here, we report the cloning of a second human homologue of Dsh (called DVL-3) by cDNA library screening. 
9344861|The human DVL-3 gene encodes a predicted 716 amino acid protein which exhibits 98% amino acid identity with mouse Dvl-3 and 49% with Drosophila Dsh. 
7958461|In the Drosophila embryo dishevelled (dsh) function is required by target cells in order to respond to wingless (wg, the homolog of Wnt-1), demonstrating a role for dsh in Wnt signal transduction. 
7958461|We have isolated a mouse homolog of the Drosophila dsh segment polarity gene. 
7958461|The 695-amino-acid protein encoded by the mouse dishevelled gene (Dvl-1) shares 50% identity (65% similarity) with dsh. 
7958461|While no functional motifs were identified, one region of Dvl-1 was found to be similar to a domain of discs large-1 (dlg), a Drosophila tumor suppressor gene.
ELIA_PHYCP.struc:
7763784|We found that Phytophthora megasperma megasperma produces two elicitin isoforms, each belonging to a different physico-chemical class, although the beta elicitin was less toxic than other beta ones. 
7763784|These 98 residue proteins were purified, sequenced and compared with other known elicitins. 
7763784|In addition to the point mutation already known to correlate with the differences in necrotic activities between alpha and beta isoforms, we found another region of the molecule likely to be involved in the regulation of the toxicity.
2776750|They are proteins of similar Mr (respectively 10,323 and 10,155) and their complete amino acid sequences were determined. 
2776750|They consist of 98 residues, with some internal repetitions of hexapeptides and heptapeptides. 
2776750|85% identity was observed between both sequences: only two short terminal regions are heterologous, while the central core is entirely conserved. 
2776750|Secondary structure predictions, hydropathy and flexibility profiles differ only around position 15 and at the C-terminus; these modifications could play a role in the modulation of their biological activities.
9385630|Cryptogein belongs to a new family of 10-kDa proteins called elicitins.
9385630|The structure of beta cryptogein reveals a novel protein fold, with five helices and a double-stranded beta-sheet facing an omega-loop.
9385630| One edge of the beta-sheet and the adjacent face of the omega-loop form a hydrophobic cavity. 
9385630|This cavity made of highly conserved residues represents a plausible binding site. 
9385630|Residue 13, which has been identified from directed mutagenesis and natural sequence comparison studies as a key amino acid involved in the differential control of necrosis, is surface exposed and could contribute to the binding to a ligand or a receptor. 
1368359|We found that Phytophthora drechsleri produces several elicitin isoforms of various toxicity on tobacco. 
1368359|The CD spectra showed that their secondary structure was largely conserved, exhibiting ca 50% alpha-helix and little or no beta-structure. 
1368359|These 98 residue proteins were sequenced and compared with other known elicitins. 
1368359|Only one point mutation correlated with the differences in necrotic activities. 
1368359|This residue could be either an active or a regulatory site, involved in the interaction with a receptor responsible for necrosis induction.
8125100|The secondary structure topology of the molecule is composed of five helices and an antiparallel beta-sheet. 
8125100|Four of the helices compose two pairs running antiparallel while the last one is parallel to the beta-sheet.
8274771|Elicitin was confirmed to be encoded as a precursor protein containing a 20-amino acid signal peptide that is processed before secretion. 
8031752|The backbone 1H and 15N resonance assignments and solution secondary structure determination of capsicein, a protein of 98 residues with a molecular mass of 10161 Da, are presented.
8031752|The data show five alpha-helical regions comprising residues 5-18, 26-33, 44-58, 59-67, and 86-98 and a two-stranded antiparallel beta-sheet involving residues 70-75 and 80-85, packed around a hydrophobic core grouping all of the aromatic residues. 
8031752|The C-terminal secondary structure motifs of capsicein evoke phospholipase structural features, which suggests that elicitins might interact with the lipidic molecules of the plasma membrane.
8994969|The overall structure has a novel fold consisting of six alpha helices and a beak-like motif, whose sequence is highly conserved within the family, composed of an antiparallel two-stranded beta sheet and an omega loop. 
8994969|This motif is assumed to be a major recognition site for a putative receptor and/or ligand. 
8994969|Two other distinct binding sites seem to be correlated to the level of necrotic activity of elicitins. 
2583277|The differences in the 3 elicitin sequences were correlated to the biological activities: 2 lysines were ascribed as the key amino acids involved in the differential control of protection with respect to necrosis.
FLGK_ECOLI.struc:
2544561|FlgH and FlgI, which are exported across the cell membrane to their destinations in the outer membrane and periplasmic space, respectively, both had typical N-terminal cleaved signal-peptide sequences. 
2544561|FlgH is predicted to have a considerable amount of beta-sheet structure, as has been noted for other outer membrane proteins. 
2544561|FlgI is predicted to have an even greater amount of beta-structure. 
2544561|FliF, as is usual for a cytoplasmic membrane protein of a procaryote, lacked a signal peptide; it is predicted to have considerable alpha-helical structure, including an N-terminal sequence that is likely to be membrane-spanning.
2544561|However, it had overall a quite hydrophilic sequence with a high charge density, especially towards its C terminus. 
2544561|The flgJ gene, immediately adjacent to flgI and the last gene of the flgB operon, encodes a flagellar protein of unknown function whose deduced sequence was hydrophilic and may correspond to a cytoplasmic protein. 
8158647|The mutations mapped to the middle of flgL, to structural gene for HAP3, and sequence analysis revealed the same coding change in both mutants: a substitution of cysteine for arginine 168. 
8158647|The N-terminal sequence of HAP3 was found to be similar to the N-terminal sequence of flagellin, and the possibility that it provides a nucleation site for the C-terminal region of flagellin is discussed.
2193164|Hook protein most strongly resembled the distal rod protein (FlgG) and the proximal HAP (HAP1), which are thought to be attached to the proximal and distal ends of the hook, respectively; the similarities were most pronounced near the N and C termini. 
2193164|Hook protein and flagellin, which occupy virtually identical helical lattices, did not resemble each other strongly but showed some limited similarities near their termini. 
2193164|HAP3 and HAP2, which form the proximal and distal boundaries of the filament, showed few similarities to flagellin, each other, or the other axial proteins.
2193164|With the exceptions of the N-terminal region of HAP2, and the C-terminal region of flagellin, proline residues were absent from the terminal regions of the axial proteins. 
2193164|Moreover, with the exception of the N-terminal region of HAP2, the terminal regions contained hydrophobic residues at intervals of seven residues. 
2193164|Together, these observations suggest that the axial proteins may have amphipathic alpha-helical structure at their N and C termini. 
2193164|In the case of the filament and the hook, the terminal regions are believed to be responsible for the quaternary interactions between subunits. 
2193164|We suggest that this is likely to be true of the other axial structures as well, and specifically that interaction between N-terminal and C-terminal alpha-helices may be important in the formation of the axial structures of the flagellum. 
2193164|Although consensus sequences were noted among some of the proteins, such as the rod, hook and HAP1, no consensus extended to the entire set of axial proteins.
GAA6_CHICK.struc:
11992121|We report that an Ala322Asp mutation in GABRA1, encoding the alpha1 subunit of the gamma-aminobutyric acid receptor subtype A (GABA(A)), is found in affected individuals of a large French Canadian family with juvenile myoclonic epilepsy.
1846404|gamma-Aminobutyric acidA (GABAA) receptors are multisubunit ligand-gated ion channels which mediate neuronal inhibition by GABA and are composed of at least four subunit types (alpha, beta, gamma, and delta). 
1846404|In cloning murine gamma 2-subunits, we isolated cDNAs encoding forms of the subunit that differ by the insertion of eight amino acids. 
1846404|LLRMFSFK, in the major intracellular loop between proposed transmembrane domains M3 and M4. 
1846404|The eight-amino-acid insertion encodes a potential consensus serine phosphorylation site for protein kinase C.
2556293|The predicted 51 amino acid long mature protein contains an exceptionally long intracellular domain and shares 53-56% sequence similarity to the previously characterized alpha 1, alpha 2 and alpha 3 subunits. 
3037384| Amino-acid sequences derived from complementary DNAs encoding the alpha- and beta-subunits of the GABA/benzodiazepine receptor from bovine brain show homology with other ligand-gated receptor subunits, suggesting that there is a super-family of ion-channel-containing receptors.
9339354|A cDNA sequence of the gene coding for a 506 amino acid protein was identified, representing a member of a putative new class (epsilon) of the GABAA receptor. 
2561977|Two cDNAs (alpha 1 and alpha 4) from rat brain cDNA libraries encode isoforms of the alpha subunit of the GABA/benzodiazepine receptor, which differ at 30% of their amino acid residues. 
2847710|The 351 amino acid sequence of this human alpha subunit shows 97% homology with its bovine counterpart.
1647983|The gamma 3 cDNA encodes a mature protein of 450 amino acids that contains structural features typically conserved among subunits of the GABAA receptor family. 
1647983|The gamma 3 subunit shares approximately 66% sequence identity with the gamma 2 subunit but only 38% and 29% with alpha 1 and beta 1 subunits, respectively.
8780005|These proteins exhibit 83 and 75% identity, respectively, to the rat alpha 6 polypeptide. 
8632757|The deduced amino acid sequence of this cDNA shows 91.4% identity with the published rat alpha 6 subunit.
8719414|Its deduced amino acid sequence shows a high level of sequence identity with the published mouse and rat sequences (96%).
1849552|Its deduced amino acid sequence is 96% identical to that of the alpha 2 polypeptide of the bovine GABAA receptor. 
1849552|The polypeptide has features shared by all previously reported GABAA receptor alpha polypeptides and shares 71-76% identity with previously described rat alpha polypeptides. 
1849552|Most of the differences lie in the presumed extracellular and intracellular domains.
9527017|The mouse gamma1-subunit complementary DNA (cDNA) shares 98% similarity with that of the rat at the level of amino acid sequence.
9084408|This channel subunit has significant amino acid identity (25-40%) with members of GABAA and GABAC receptor subunits and thus may represent a new subfamily of the GABA receptor channel.
2538761|This heterooligomeric receptor exists in most inhibitory synapses in the vertebrate central nervous system (CNS) and can be regulated by clinically important compounds such as benzodiazepines and barbiturates. 
2538761|We now report the isolation of a cloned cDNA encoding a new GABAA receptor subunit, termed gamma 2, which shares approximately 40% sequence identity with alpha- and beta-subunits and whose messenger RNA is prominently localized in neuronal subpopulations throughout the CNS.
2157817|A cDNA encoding a protein with 70% amino acid identity to the previously characterized gamma-aminobutyric acidA (GABAA) receptor alpha-subunits was isolated from a rat brain cDNA library by homology screening.
1702226|Two forms of bovine gamma 2 subunit cDNA were isolated (gamma 2S and gamma 2L) that differed by the presence or absence of a 24-base-pair (8-amino acid) insertion in the cytoplasmic domain between the third and fourth putative membrane-spanning regions. 
1702226|Analysis of the sequence of the 8-amino acid insert revealed that it contains a protein kinase C consensus phosphorylation site. 
1702226|Expression of the large cytoplasmic loop domains of gamma 2S and gamma 2L in Escherichia coli, followed by phosphorylation of the recombinant proteins by protein kinase C, demonstrated that gamma 2L, but not gamma 2S, could be phosphorylated.
1702226|Thus the two forms of gamma 2 subunit differ by the presence or absence of a protein kinase C phosphorylation site. 
9892355|Type-A receptors for the neurotransmitter GABA (gamma-aminobutyric acid) are ligand-gated chloride channels that mediate inhibitory neurotransmission.
1702226|Each subunit of the pentameric receptor protein has ligand-binding sites in the amino-terminal extracellular domain and four membrane-spanning regions, one of which forms a wall of the ion channel.
1702226|Each subunit also has a large intracellular loop that may be a target for protein kinases and be required for subcellular targeting and membrane clustering of the receptor, perhaps by anchoring the receptor to the cytoskeleton. 
1702226|Sequence analysis shows similarity between GABARAP and light chain-3 of microtubule-associated proteins 1A and 1B. 
1702226|Moreover, the N terminus of GABARAP is highly positively charged and features a putative tubulin-binding motif.
2561970|These subunits, gamma 2 and delta, share approximately 35% sequence identity with alpha and beta subunits and form functional GABA-gated chloride channels when expressed alone in vitro. 
2561970|The gamma 2 subunit is the rat homolog of the human gamma 2 subunit recently shown to be important for benzodiazepine pharmacology. 
8391122|Their deduced amino acid sequences show much sequence identity with the published bovine sequences (98.2% and 97.0% for alpha 2 and alpha 3, respectively). 
1848528|The cDNA is 2665 nucleotides long with an open reading frame of 455 amino acids. 
1848528|It shows significant homology to the GABAA receptor alpha 1 subunit cDNA sequences of other species.
1848528|Excluding deletions, the murine GABAA alpha 1 receptor exhibits 96% nucleotide and 100% amino acid sequence homology to the rat alpha 1 receptor cDNA and over 91% nucleotide and 98% amino acid sequence homology to the bovine and human alpha 1 receptor cDNAs in the protein coding region. 
2170110|Both gamma subunit variants share 74% sequence similarity and are prominently synthesized in often distinct areas of the central nervous system as documented by in situ hybridization. 
8397108|The mature polypeptide (which we name gamma 4) displays 67%, 69% and 70% identity, respectively, to the rat gamma 1, gamma 2 and gamma 3 subunits. 
2465923|The human subunits display very high levels of sequence identity with the corresponding bovine receptor subunits.
HH1R_BOVIN.struc:
8294913|It encodes a protein of 488 amino acids with a calculated molecular mass of 55,619 daltons compared with a size of 56-68 kDa for the photoaffinity-labeled receptor as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. 
8294913|The protein displays a 66% homology with the bovine receptor.
8280179|The deduced protein of 487 amino acids showed characteristic properties of G-protein-coupled receptors. 
7678492|The receptor protein deduced from this isolated gene was composed of 486 amino acids and showed characteristic properties of G protein-coupled receptors. 
1722337|The H1 receptor cDNA encodes a protein of 491 amino acids (Mr 55,954) with seven putative transmembrane domains, illustrating the similarity to other receptors that couple with guanine nucleotide-binding regulatory proteins (G protein-coupled receptors). 
1722337|The sequence homology between the H1 and H2 receptors is not higher than that between the histamine H1 and m1-muscarinic receptors. 
8812432|The protein deduced from the nucleotide sequence is composed of 488 amino acid residues with characteristic properties of GTP binding protein-coupled receptors.
8282735|The gene contains no introns and encodes a protein of 488 amino acid residues. 
8282735|The structure of the guinea-pig histamine H1 receptor is predicted to contain seven putative transmembrane regions, which are similar to those of receptors coupling with GTP binding proteins. 
8282735|Although the third intracellular domain, the predicted binding site for the GTP binding protein, showed only 50% identity with those of the bovine and rat H1 receptors, the expressed guinea-pig H1 receptor was fully able to bind with [3H]mepyramine. 
8003029|The receptor protein deduced from the nucleotide sequence of this gene was composed of 487 amino acid residues with a calculated Mr of 55,781 and possessed characteristic properties of GTP binding protein-coupled receptors.
HUGA_VESVU.struc:
8828537|Yellow jacket antigen 5 has been previously cloned and expressed in bacteria; it contains 204 amino acid residues, and it has 69% and 60% sequence identities with the homologous proteins of white-faced hornet (Dolichovespula maculata) and wasp (Polistes annularis), respectively. 
8828537|These studies are now extended to yellow jacket hyaluronidase and phospholipase; they contain 331 and 300 amino acid residues, respectively, and they show 92% and 67% sequence identity with their homologs of white-faced hornet. 
7876212|We have cloned Dol m 2, a protein of 331 residues. When expressed in bacteria, a mixture of recombinant Dol m 2 and its fragments was obtained. 
7876212|The fragments were apparently generated by proteolysis of a Met-Met bond at residue 122, as they were not observed for a Dol m 2 mutant with a Leu-Met bond. 
7876212|Dol m 2 has 56% sequence identity with the honey bee venom allergen hyaluronidase and 27% identity with PH-20, a human sperm protein with hyaluronidase activity. 
7876212|A common feature of hornet venom allergens is their sequence identity with other proteins in our environment. 
7876212|We showed previously the sequence identity of Dol m 5 with a plant protein and a mammalian testis protein and of Dol m 1 with mammalian lipases.
KBF2_HUMAN.struc:
9450761|The NF-kappaB p50/p65 heterodimer is the classical member of the Rel family of transcription factors which regulate diverse cellular functions such as immune response, cell growth, and development. 
9450761|Other mammalian Rel family members, including the proteins p52, proto-oncoprotein c-Rel, and RelB, all have amino-terminal Rel-homology regions (RHRs).
9450761|The RHR is responsible for the dimerization, DNA binding and cytosolic localization of these proteins by virtue of complex formation with inhibitor kappaB proteins. 
9450761|This structure indicates why the p50/p65 heterodimer interface is stronger than that of either homodimer. 
9450761|A comparison of this structure with those of other Rel dimers reveals that both subunits adopt variable conformations in a DNA-sequence-dependent manner. 
9450761|Our results explain the different behaviour of the p50/p65 heterodimer with heterologous promoters.
9865694|IkappaBalpha regulates the transcription factor NF-kappaB through the formation of stable IkappaBalpha/NF-kappaB complexes. 
9865694|The 2.3 A crystal structure of IkappaBalpha in complex with the NF-kappaB p50/p65 heterodimer reveals mechanisms of these inhibitory activities. 
9865694|The presence of IkappaBalpha allows large en bloc movement of the NF-kappaB p65 subunit amino-terminal domain. 
9865694|Amino acid residues immediately preceding the nuclear localization signals of both NF-kappaB p50 and p65 subunits are tethered to the IkappaBalpha amino-terminal ankyrin repeats, impeding NF-kappaB from nuclear import machinery recognition.
1339305|The deduced 607 amino acid sequence is identical to the sequence of the C-terminal region of 110 kd NF-kappa B protein. 
1339305|A 70 kd protein can be identified in lymphoid cells using antibodies raised against the C-terminal region of p110 NF-kappa B. 
1339305|Comparison of the two-dimensional tryptic peptide maps of the 70 kd protein expressed in cells and the in vitro translated product encoded by the cDNA display extensive homology. 
1339305|The 70 kd protein expressed in bacteria prevents sequence-specific DNA binding of p50-p65 NF-kappa B heterodimer, p50 homodimer, and c-rel.
1339305|The 70 kd protein, predominantly found in lymphoid cells, is a new member of the I kappa B family of proteins and is referred to as I kappa B gamma.
9529257|p50 corresponds to the N terminus of p105 and with p65 (RelA) forms the prototypical NF-kappaB transcription factor complex. 
9950430|The transcription factor NF-kappaB is composed of homodimeric and heterodimeric complexes of Rel/NF-kappaB-family polypeptides, which include Rel-A, c-Rel, Rel-B, NF-kappaB/p50 and NF-kappaB2/p52 . 
9950430|The NF-kappaB1 gene encodes a larger precursor protein, p105, from which p50 is produced constitutively by proteasome-mediated removal of the p105 carboxy terminus. 
9950430|Following cell stimulation by agonists, p105 is proteolysed more rapidly and released Rel subunits translocate into the nucleus. 
9950430|Here we show that TPL-2 , which is homologous to MAP-kinase-kinase kinases in its catalytic domain, forms a complex with the carboxy terminus of p105. 
9950430|TPL-2 was originally identified, in a carboxy-terminal-deleted form, as an oncoprotein in rats and is more than 90% identical to the human oncoprotein COT. 
9950430|This releases associated Rel subunits or p50-Rel heterodimers to generate active nuclear NF-kappaB.
9865693|The structure of the IkappaBalpha ankyrin repeat domain, bound to a partially truncated NF-kappaB heterodimer (p50/ p65), has been determined by X-ray crystallography at 2.7 A resolution. 
9865693|It shows a stack of six IkappaBalpha ankyrin repeats facing the C-terminal domains of the NF-kappaB Rel homology regions. 
9865693|Contacts occur in discontinuous patches, suggesting a combinatorial quality for ankyrin repeat specificity. 
9865693|The first two repeats cover an alpha helically ordered segment containing the p65 nuclear localization signal.
 9865693|The position of the sixth ankyrin repeat shows that full-length IkappaBalpha will occlude the NF-kappaB DNA-binding cleft. 
1531086|The cDNA has an open reading frame of 900 amino acids capable of encoding a 97-kDa protein. 
1531086|This protein is most similar to the 105-kDa precursor polypeptide of p50-NF-kappa B. 
1531086|Like the 105-kDa precursor, it contains an amino-terminal Rel-related domain of about 300 amino acids and a carboxy-terminal domain containing six full cell cycle or ankyrin repeats. 
1531086|p50B is able to form heteromeric kappa B-binding complexes with RelB, as well as with p65 and p50, the two subunits of NF-kappa B. 
7510259|NF-kappa B is a transcription factor composed of the p50 and p65 subunits. 
7510259|The deduced amino acid sequence of the precursor protein, p97, shows conservation of the overall structure, and 86% identity in the Rel homology domain (RHD) and 56% identity in the ankyrin repeat domain (ARD) to human p50B/p97. 
1533881|Active NF-kappa B-like transcription complexes are multimers consisting of one or two members of a family of proteins related to the c-Rel proto-oncoprotein.
1533881|We have isolated a chicken cDNA encoding p105, the precursor protein for the p50 subunit of NF-kappa B. 
1533881|Sequence analysis shows that chicken p105 is approximately 70% identical to the mouse and human p105 proteins, containing the Rel homology domain in its N-terminal 370 amino acids and several ankyrinlike repeats in the C-terminal portion of the protein.
1533881| The Rel homology domain is particularly highly conserved between chicken and mammalian p50, and an in vitro-synthesized, truncated chicken p105 protein, containing sequences that correspond to the predicted p50 protein, bound to a consensus kappa B site in an electrophoretic mobility shift assay.
1533881|In v-Rel-transformed chicken spleen cells, v-Rel is found in high-molecular-weight complexes which include cellular proteins of approximately 124 kDa (p124) and 115 kDa (p115). 
1992489|The DNA binding subunit of nuclear factor kappa B (NF-kappa B), a B-cell protein that interacts with the immunoglobulin kappa light-chain gene enhancer, has been purified from nuclei of human HL-60 cells stimulated with tumor necrosis factor alpha (TNF alpha), and internal peptide sequences were obtained. 
1992489|The encoded open reading frame of about 105 kDa contained at its N-terminal half all six tryptic peptide sequences, suggesting that the 51-kDa NF-kappa B protein is processed from a 105-kDa precursor. 
1992489|This region also showed high homology to a domain shared by the Drosophila dorsal gene and the avian and mammalian rel (proto)oncogene products. 
7969179|The NF-kappa B1 subunit of the transcription factor NF-kappa B is derived by proteolytic cleavage from the N terminus of a 105-kDa precursor protein. 
7969179|The C terminus of p105NF-kappa B1, like those of I kappa B proteins, contains ankyrin-related repeats that inhibit DNA binding and nuclear localization of the precursor and confer I kappa B-like properties upon p105NF-kappa B1. 
7969179|Here we report the characterization of two novel NF-kappa B1 precursor isoforms, p84NF-kappa B1 and p98NF-kappa B1, that arise by alternate splicing within the C-terminal coding region of murine nfkb1. 
7969179|p98NF-kappa B1, which lacks the 111 C-terminal amino acids (aa) of p105NF-kappa B1, has a novel 35-aa C terminus encoded by an alternate reading frame of the gene.
7969179|p84NF-kappa B1 lacks the C-terminal 190 aa of p105NF-kappa B1, including part of ankyrin repeat 7. 
7969179|Transient transfection analysis revealed that p98NF-kappa B1, but not p105NF-kappa B1 or p84NF-kappa B1, acts as a transactivator of NF-kappa B-regulated gene expression and that this is dependent on sequences in the Rel homology domain required for DNA binding and on the novel 35 C-terminal aa of this isoform.
7969179|In contrast to previous findings, which indicated that p105NF-kappa B1 does not bind DNA, all of the NF-kappa B1 precursors were found to specifically bind with low affinity to a highly restricted set of NF-kappa B sites in vitro, thereby raising the possibility that certain of the NF-kappa B1 precursor isoforms may directly modulate gene expression.
9384558|Members of this family of proteins form homo- and heterodimers with differing affinities for dimerization. 
9384558|They share a structural motif known as the rel homology region (RHR), the C-terminal one third of which mediates protein dimerization. 
9384558|These structures showed that the residues from the dimerization domains of both p50 and p65 participate in DNA binding and that the DNA-protein and protein dimerization surfaces form one continuous overlapping interface.
9384558|We desired to investigate the contribution of DNA to NFkappaB dimerization and to identify the mechanism for the selective association of rel/NFkappaB family peptides into transcriptionally active dimers.
9384558|RESULTS: We report here the crystal structures of the dimerization domains of murine p50 and p65 at 2.2 A and 2.0 A resolution, respectively.
9384558|A comparison of these two structures suggests that conservative amino acid changes at three positions are responsible for the differences in their dimer interfaces. 
9384558|The presence of the target DNA does not change the dimer interface of either protein in any significant manner. 
9384558|CONCLUSIONS: These two structures suggest that the rel/NFkappaB family of transcription factors use only a few conservative changes in their amino acid sequences to form a host of dimers with varying affinities for dimerization. 
9384558|The DNA-contacting charged amino acid sidechains from the dimerization domains are held in a similar conformation in both the DNA-bound and free states, therefore, no major structural rearrangement is required to bring these residues into contact with the DNA.
2203531|We have isolated a complementary cDNA coding for KBF1 and identified the DNA binding and dimerization domain of the protein. 
2203531|It appeared that KBF1 is, by all criteria used, identical to the 50 kd DNA binding subunit of NF-kappa B. KBF1 (and therefore p50) also displays extensive amino acid sequence homology with the v-rel oncogene and the Drosophila maternal morphogen dorsal. 
8036016|We have identified a rearrangement of the NFKB-2 gene in the HUT 78 human cutaneous T-cell leukemia (CTCL) line, cDNA and genomic DNA sequence predicted the presence of a truncated 80 kD NFKB-2 precursor protein (p80HT), instead of the normal p100 protein. 
7830764|The structure of a large fragment of the p50 subunit of the human transcription factor NF-kappa B, bound as a homodimer to DNA, reveals that the Rel-homology region has two beta-barrel domains that grip DNA in the major groove. 
7830764|The amino-terminal specificity domain contains a recognition loop that interacts with DNA bases; the carboxy-terminal dimerization domain bears the site of I-kappa B interaction.
7830764|The folds of these domains are related to immunoglobulin-like modules. 
7830764|The amino-terminal domain also resembles the core domain of p53.
8825636|We propose that the long size of NFKB1 is important for transient activation of NF-kappa B complexes containing p50. 
8825636|I kappa B-gamma corresponds to the carboxyl-terminal half of p105.
8230480|Full-length p100 only weakly binds DNA in vitro; removal of the ankyrin-like repeats generates C-terminally truncated p100 proteins (like p52) that have an increased ability to bind an oligonucleotide containing a kappa B site. 
10469655|p50 homodimers are specifically bound by the transcription activator Bcl-3. 
10469655|The IkappaB kinases IKKalpha and IKKbeta physically interact with p105 and inducibly phosphorylate three C-terminal serines. 
10469655|Thus, the known NF-kappaB stimuli not only cause nuclear accumulation of p50-p65 heterodimers but also of Bcl-3-p50 and perhaps further transcription activator complexes which are formed upon IKK-mediated p105 degradation.
9384586|Whereas the overall structure resembles that of the NF-kappaB p50-DNA complex, pronounced differences are observed within the 'insert region'.
9384586|This sequence segment differs in length between different Rel proteins. 
9384586|Compared with NF-kappaB p50, the compact alpha-helical insert region element is rotated away from the core of the N-terminal domain, opening up a mainly polar cleft. 
9384586|The high resolution of the structure reveals many water molecules which mediate interactions in the protein-DNA interface.
9384586|Additional complexity in Rel protein-DNA interaction comes from an extended interfacial water cavity that connects residues at the edge of the dimer interface to the central DNA bases. 
9384586|The observed water network might acount for differences in binding specificity between NF-kappaB p52 and NF-kappaB p50 homodimers.
8087845|The p105 precursor of the p50 subunit of NF-kappa B is processed in vitro by an ATP-dependent process that requires proteasomes and ubiquitin conjugation. 
8087845|The C-terminal region of p105 is rapidly degraded, leaving the N-terminal p50 domain. 
7530332|The 2.3-A crystal structure of the transcription factor NK-kappa B p50 homodimer bound to a palindromic kappa B site reveals that the Rel homology region folds into two distinct domains, similar to those in the immunoglobulin superfamily. 
7530332|The p50 dimer envelopes an undistorted B-DNA helix, making specific contacts along the 10-base-pair kappa B recognition site mainly through loops connecting secondary structure elements in both domains. 
7530332|The carboxy-terminal domains form a dimerization interface between beta-sheets using residues that are strongly conserved in the Rel family.
8398903|The p50 subunit of NF-kappa B is derived from the amino terminus of a 105 kilodalton precursor. 
8398903|The p105 carboxyl terminus, which contains ankyrin-like repeats, a feature of I kappa B molecules, regulates the cytoplasmic retention of p105 and inhibits DNA binding by the precursor. 
8398903|Here, we describe an I kappa B protein identical to the carboxyl-terminal region of p105. 
8398903|Probes spanning the COOH terminus but not the rel homology domain of p105 hybridize to a distinct 2.6-kilobase mRNA expressed in a wide range of murine tissues.
8398903|The nucleotide sequence of complementary DNA clones for this transcript, in vitro translation, and immune precipitation of metabolically labeled cell lysates establish that it encodes a 70 kilodalton protein that corresponds to the COOH-terminal 607 amino acids of p105. 
8398903|p70 suppresses p65 and p75c-rel mediated transactivation of reporter genes under the control of NF-kappa B elements and in vitro can prevent DNA binding of p50 and p75c-rel homodimers to NF-kappa B sites. 
1876189|The transcription factor NF-kappa B is a protein complex which comprises a DNA-binding subunit and an associated transactivation protein (of relative molecular masses 50,000 (50K) and 65K, respectively). 
1876189|Both the 50K and 65K subunits have similarity with the rel oncogene and the Drosophila maternal effect gene dorsal. 
1876189|The 50K DNA-binding subunit was previously thought to be a unique protein, derived from the 105K gene product (p105).
1876189| We now report the isolation of a complementary DNA that encodes an alternative DNA-binding subunit of NF-kappa B.
1876189|It is synthesized as approximately 100K protein (p100) that is expressed in different cell types, contains cell cycle motifs and, like p105, must be processed to generate a 50K form.
1876189|A 49K product (p49) can be generated independently from an alternatively spliced transcript; it has specific kappa B DNA-binding activity and can form heterodimers with other rel proteins.
2203532|The DNA binding subunit of the transcription factor NF-kappa B, p50, has been cloned. 
2203532|Sequence analysis reveals remarkable homology for over 300 amino acids at the amino-terminal end to the oncogene v-rel, its cellular homolog c-rel, and the Drosophila maternal effect gene dorsal. 
2203532|However, p65 appears homologous to c-rel, suggesting that c-rel may form heterodimers with p50 and rel may include a homodimerization motif.
11297557|The p105 PEST domain contains a motif (Asp-Ser(927)-Gly-Val-Glu-Thr), related to the IKK target sequence in IkappaBalpha, which is conserved between human, mouse, rat, and chicken p105. 
11297557|Analysis of a panel of human p105 mutants in which serine/threonine residues within and adjacent to this motif were individually changed to alanine established that only serine 927 is essential for p105 proteolysis triggered by IKK2 overexpression. 
11297557|Together these experiments indicate that the IKK complex regulates the signal-induced proteolysis of NF-kappaB1 p105 by direct phosphorylation of serine 927 in its PEST domain.
OTX2_BRARE.struc:
7720578|The presence of the Xotx2 homeodomain is required to produce these effects. 
7720578|In particular, this homeodomain contains a specific lysine residue at position 9 of the recognition helix. 
7720578|Microinjected transcripts of Xotx2 constructs containing a homeodomain where this lysine is substituted by a glutamine or a glutamic acid residue fail to cause these effects.
7898305|Three zebrafish otx homeoproteins containing a homeodomain homologous to that of the Drosophila orthodenticle head gap gene product have been identified by cloning and sequencing of cDNAs. 
7898305|The zebrafish otx2 homeoprotein shares high amino-acid sequence identity with the mouse Otx2 homeoprotein, whereas the zebrafish otx1 and otx3 homeoproteins exhibit moderate homology with the mouse Otx1 and Otx2 homeoproteins. 
7893604|zOtx1 and zOtx2 encode predicted gene products which are 82% and 94% identical to the corresponding mouse proteins.
8101484|Its gene product contains a homeodomain of the bicoid class and is able to recognize and transactivate a bicoid target sequence.
PENK_XENLA.struc:
7057924|The corresponding amino acid sequence shows that the precursor is 267 amino acids long and contains six interspersed Met-enkephalin sequences and one Leu-enkephalin sequence. 
7057924|Five of the seven enkephalins are flanked on both sides by pairs of basic amino acid residues. 
9126357|Mass spectrometry of fragments produced by limited proteolytic digestion of pro-enkephalin was used to locate the disulfide bridges in synenkephalin (pro-enkephalin 1-73), a domain which contains sorting information for targeting the pro-neuropeptide to the granules of the regulated secretory pathway in neuroendocrine cells. 
9126357|Three disulfide bridges between Cys2-Cys24, Cys6-Cys28, and Cys9-Cys41 were identified. 
9126357|Protein conformational prediction of synenkephalin1-42 shows beta-turns which facilitate the formation of these disulfide bonds.
PRO2_HUMAN.struc:
7758455|We refer to this recently described isoform as profilin II (isoelectric point 5.9) in comparison to profilin I (pI 8.4).
7601111|We purified profilin from bovine brain and were able to separate the two isoforms present in this tissue. 
8365484|We have isolated a 1.7 kbp cDNA encoding a 140 amino acid protein (15.1 kDa, pI 5.91) with a high sequence similarity (62%) to human profilin (profilin I). 
11027290|Two transcripts encode different profilin II isoforms (designated IIa and IIb) that have similar affinities for actin but different affinities for polyphosphoinositides and proline-rich sequences. 
11027290|Profilins IIa and IIb are also present in humans, suggesting that all mammals have three profilin isoforms. 
10600384|Human profilins are multifunctional, single-domain proteins which directly link the actin microfilament system to a variety of signalling pathways via two spatially distinct binding sites.
10600384|Profilin binds to monomeric actin in a 1:1 complex, catalyzes the exchange of the actin-bound nucleotide and regulates actin filament barbed end assembly. 
10600384|Like SH3 domains, profilin has a surface-exposed aromatic patch which binds to proline-rich peptides. 
10600384|Various multidomain proteins including members of the Ena/VASP and formin families localize profilin:actin complexes through profilin:poly-L-proline interactions to particular cytoskeletal locations (e.g. focal adhesions, cleavage furrows).
10600384|Humans express a basic (I) and an acidic (II) isoform of profilin which exhibit different affinities for peptides and proteins rich in proline residues. 
10600384|This structure reveals an aromatic extension of the previously defined poly-L-proline binding site for profilin I. 
10600384|In contrast to serine 29 of profilin I, tyrosine 29 in profilin II is capable of forming an additional stacking interaction and a hydrogen bond with poly-L-proline which may account for the increased affinity of the second isoform for proline-rich peptides. 
10600384|Differential isoform specificity for proline-rich proteins may be attributed to the differences in charged and hydrophobic residues in and proximal to the poly-L-proline binding site. 
10600384|The actin-binding face remains nearly identical with the exception of five amino acid differences.
10600384|These observations are important for the understanding of the functional and structural differences between these two classes of profilin isoforms.
RBS_TOBAC.struc:
3478552|We have cloned and sequenced all five members of the gene family for the small subunit (rbcS) of ribulose-1,5-bisphosphate carboxylase/oxygenase from tomato, Lycopersicon esculentum cv. VFNT LA 1221 cherry line. 
3557127|We have isolated and sequenced two cDNA clones (LESS5 and LESS17) encoding the small subunit of ribulose-1,5-bisphosphate carboxylase of tomato (Lycopersicon esculentum).
8299958|We determined the nucleotide sequences of five members of the rbcS gene family encoding the small subunit (SSU) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) of potato. 
8425051|DNase I footprinting assays were used to map sites of DNA-protein interaction in the promoter regions of three of the five genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase (rbcS) in tomato.
4000958|We have cloned and sequenced a gene for the small subunit (SS) of ribulose bis-phosphate carboxylase-oxygenase from Nicotiana tabacum.
4000958|The tobacco gene is most closely related to the SS genes from the dicots soybean and pea, and less so to the monocots wheat and Lemna; the deduced amino acid sequence of the mature protein is in all cases more closely conserved than is its chloroplast transit sequence. 
4000958|The third tobacco intron lies within a highly conserved region of the protein. 
4000958|Its position coincides with the boundary of a 12 amino acid insertion in the SS genes of higher plants, relative to those of blue green algae.
1512238|The refined model consists of residues 22-63 and 69-467 of the large subunit and the complete small subunit. 
1512238|A striking feature of the model is that several loops have very high B-factors, probably representing mobile regions of the molecule. 
1512238|An examination of the intersubunit contacts shows that the L8S8 hexadecamer is composed of four L2 dimers. 
1512238|The dominant contacts between these L2 dimers are formed by the small subunits. 
1512238|This suggests that the small subunits may be essential for maintaining the integrity of the L8S8 structure. 
1512238|The active site shows differences between the unactivated form and the quaternary complex. 
1512238|In particular, Lys334 has moved out of the active site by about 10A. 
1512238|This residue lies on loop 6 of the alpha beta barrel, which is a particularly mobile loop. 
1512238|The site of ribulose-1,5-bisphosphate carboxylase/oxygenase activation is well ordered in the absence of the carbamylation of Lys201 and Mg2+ binding.
1512238|The residues are held poised by a network of hydrogen bonds.
3012537|The nuclear gene sequences encoding RBCS, the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) from several plants show extensive interspecific divergence but little intraspecific divergence, suggesting that these genes are evolving in concert within a genome. 
3012537|However, the mature part of the polypeptide encoded by the tobacco RBCS gene differs by five and six amino acids from the corresponding region in the polypeptides encoded by Rbcs-2A and Rbcs-3A, respectively, while these two tomato RBCS polypeptides differ from each other in the mature part by a single amino acid.
3012537|Rbcs-1, whose nucleotide sequence shows higher divergence from both the tobacco RBCS gene and Rbcs-2A and Rbcs-3A, encodes a polypeptide whose mature part differs by eight amino acids from the corresponding region in the tobacco polypeptide but only by three and four amino acids from the corresponding regions of Rbcs-2A- and Rbcs-3A-encoded polypeptides, respectively.
3684569|Genomic clones containing three genes for the small subunit (SSU) of ribulose bisphosphate carboxylase were isolated from tobacco. 
6549380|The combination of cDNA and RNA sequencing techniques has enabled determination of the complete sequence of one of the mRNAs coding for the precursor of the small subunit of ribulose bisphosphate carboxylase of Nicotiana sylvestris.
6549380|In this 898-nucleotide-long mRNA, 540 nucleotides code for the entire 180-amino-acid-long precursor polypeptide consisting of the 57-amino acid-long transit peptide and the 123-amino-acid-long mature protein, while 60 and 195 nucleotides belong to the 5' and 3' noncoding flanking regions, respectively. 
SEP7_HUMAN.struc:
9022087|GP Ib is composed of two subunits (GP Ib(alpha) and GP Ib(beta)) each synthesized from separate genes. 
9022087|The 206 amino acid precursor of GP Ib(beta) is synthesized from a 1.0-kb mRNA expressed by megakaryocytes and was originally characterized from cDNA clones of human erythroleukemic (HEL) cell mRNA, a cell line exhibiting megakaryocytic-like properties. 
9022087|This newly identified 5' gene contains an open reading frame encoding 369 amino acids with a high degree of sequence similarity to an expanding family of GTP-binding proteins.
8697812|We have isolated a novel human cDNA that encodes a protein homologous to murine H5 and Diff6, and to yeast CDC10, and mapped it to chromosome region 2q37 by fluorescent in situ hybridization. 
8697812|Its transcript has an open reading frame of 1,218 nucleotides encoding 406 amino acids. 
8697812|The deduced peptide sequence contained conserved domains rich in basic residues, GXXGXGKS--DXXG--TKXD, a motif of the GTPase superfamily. 
8152419|Not surprisingly, DNA sequence analysis reveals that the proteins share extensive homology at the amino acid level with their respective S. cerevisiae counterparts.
8152419|A database search revealed significant sequence similarity with two peptides, one from Drosophila and one from mouse, suggesting strong evolutionary conservation of function.
11322766|We could show that the tag corresponds to the 3' untranslated region of this novel gene named septin 3 and cloned three isoforms A (2191 bp), B (4378 bp), and C (1896 bp) from human Ntera2/D1 cDNA.
8590280|A stretch of 10 amino acid-residues was repeated 21 times in KIAA0139, and a homologous sequence of 76-78 nucleotides was found repeated 6 times in the untranslated region of KIAA0125.
9385360|The predicted protein has P-loop nucleotide binding and GTPase motifs.
8037772|We isolated a novel human cDNA, termed hCDC10, whose predicted product showed a high degree of homology to the CDC10 protein of Saccharomyces cerevisiae. 
8037772|This cDNA contained an open reading frame of 1254 nucleotides encoding 418 amino acids, which included a GTP-binding motif, GX4GKS--DX2G--KXD.
8037772|The predicted peptide sequence also revealed partial amino-acid identity (40-50%) with Diff 6 in Drosophila and with H5 in mouse. 
8037772|Each of these sequence homologues, including Saccharomyces cerevisiae CDC10, contains the GTP-binding motif.
2174398|The nucleotide sequence of this clone predicts a relatively hydrophilic protein characteristic of a cytoplasmic or nuclear protein. 
9611266|Septins are a family of highly conserved filament-forming proteins that have been shown to mediate cytokinesis and cytoskeletal organization in fungi and Drosophila.
STRP_STREQ.struc:
8746458|This sequence coding for a 441 amino acid protein is well conserved among streptococcus species: there are two very conserved domains separated by a more variable region.
6760891|The protein consists of 415 amino acid residues. 
6760891|The NH2-terminal 245 residues of streptokinase are homologous to the sequences of several serine proteases including bovine trypsin and Streptomyces griseus proteases A and B.
6760891|The sequence alignment suggests that the active-site histidine-57 has changed to a glycine in streptokinase. 
6760891|The other active-site residues, aspartyl-102 and serine-195, are, however, present at the expected positions. 
6760891|Streptokinase also contains internal sequence homology between the NH2-terminal 173 residues and a COOH-terminal 162-residue region between residues 254 and 415. 
6760891|Moderate homology in predicted secondary structures also exists between these two regions. 
6760891|A COOH-terminal region of about 80 residues is apparently deleted from the second half of the duplicated structures. 
6760891|These observations further suggest that the three-dimensional structure of streptokinase likely contains two independently folded domains, each homologous to serine proteases.
2989113|The protein is synthesized with a 26-amino acid residue N-terminal extension having properties characteristic of a signal peptide. 
2989113|Comparison of the deduced amino acid sequence with the available amino acid sequence of a commercial streptokinase reveals minor primary structure differences. 
2989113|The nucleotide sequencing of skc does not support the hypothesis that the gene has evolved by duplication and fusion, as suggested by internal twofold amino acid homologies of its product. 
TGR3_RAT.struc:
1657407|The encoded receptor is an 853 amino acid protein with a large N-terminal extracellular domain containing at least one site for glycosaminoglycan addition, a single hydrophobic transmembrane domain, and a 41 amino acid cytoplasmic tail with no obvious signaling motif.
1657407|Introduction of the cDNA into COS cells and L6 myoblasts induces expression of a heterogenously glycosylated 280-330 kd protein characteristic of the type III receptor that binds TGF-beta 1 specifically. 
8370410|Sequencing of the largest clone (3073 bp), revealed that the leader sequence contains 25 residues and that the 586 amino acids of the extracellular and transmembrane domains were identical to those described for endothelial endoglin. 
8370410|However, the cytoplasmic tail encoded by this cDNA clone contains only 14 amino acids as opposed to the 47 residues previously reported, suggesting the existence of two alternative endoglin variants. 
8370410|The expression of these isoforms was demonstrated by polymerase chain reaction analyses on endothelial cells, myelomonocytic cell lines HL-60 and U-937, and placenta. 
8370410|Both forms were shown to bind TGF-beta 1 and, when overexpressed in transfected mouse fibroblasts, to form disulfide-linked homodimers, indicating that the cysteine residues present in the extracellular domain are responsible for the dimerization.
8294451|Human endoglin is a dimeric protein that binds transforming growth factor-beta (TGF-beta). 
8294451|The deduced sequence of the primary translated product of endoglin consists of 643 amino acids with a high sequence identity (96%) to human endoglin in the transmembrane and intracellular domains, but with a lower sequence similarity (66%) in the extracellular domain.
8294451|In contrast to human endoglin, porcine endoglin has no Arg-Gly-Asp tripeptide in its sequence. 
8294451|Antibodies, raised against a peptide corresponding to the intracellular domain of porcine endoglin, immunoprecipitated an 84-kDa protein under reducing condition and a 130-kDa protein under nonreducing condition in porcine aortic endothelial cells. 
8294451|Thus, endoglin and TGF-beta receptors I and/or II most likely formed a heteromeric receptor complex. 
8294451|These results revealed that endoglin is a phosphorylated protein which forms a heteromeric complex with signaling receptors for TGF-beta.
10545596|ENDOGLIN codes for a homodimeric membrane glycoprotein that interacts with receptors for members of the TGF-beta superfamily and is the gene mutated in the autosomal dominant vascular disorder hereditary hemorrhagic telangiectasia type 1 (HHT1). 
10545596|Here we report the analysis of four proteins resulting from point mutations, with missense codons G52V and C53R in exon 2, W149C in exon 4 and L221P in exon 5. 
8125301|The sequence of a cDNA encoding the cell surface MJ7/18 antigen revealed homology to human endoglin, a homodimeric transforming growth factor-beta (TGF-beta)-binding cell-surface glycoprotein expressed predominantly on vascular endothelial cells.
8125301|The mouse endoglin is a type-I integral membrane protein of 653 amino acids (aa). 
8125301|The human and mouse sequences display 71% aa sequence identity with almost identical transmembrane and cytoplasmic domains.
8125301|Like its human counterpart, mouse endoglin displays significant sequence homology to the type-III TGF-beta receptor in two extracellular domains, as well as striking similarity in the transmembrane and cytoplasmic regions.
8125301|One of the extracellular regions of homology with TGF-beta receptor III represents a truncated version of a homology unit defining a novel gene family including uromodulin, the pancreatic granule protein gp2, and zona pellucida receptors for sperm. 
8125301|However, unlike its human counterpart, mouse endoglin does not contain an RGD tripeptide which has been suggested as a ligand of integrins.
1333192|The human TGF-beta type III receptor coding region encodes a protein of 849 amino acids with a single transmembrane domain and a short stretch of the intracellular domain.
1333192|Potential glycosaminoglycan attachment sites were found in the extracellular domain. 
1333192|The overall amino acid sequence identities with those of the porcine and rat TGF-beta type III receptors were 83% and 81%, respectively.
1333192|A high degree of sequence conservation was observed in the transmembrane and intracellular domains, which also have sequence similarity with human endoglin. 
1333192|In addition, two portions with 29 and 52 amino acids in the extracellular domain were found to be substantially similar with human endoglin.
1657406|As deduced from its cDNA sequence, the 853 amino acid core protein of betaglycan has an extracellular domain with clustered sites for potential attachment of glycosaminoglycan chains. 
1657406|These chains are dispensable for TGF-beta binding to the core protein.
1657406|The transmembrane region and the short cytoplasmic tail of betaglycan are very similar to these regions in human endoglin, an endothelial cell membrane glycoprotein involved in intercellular recognition. 
1657406|The ectodomain of betaglycan can be released as a soluble proteoglycan; a potential cleavage site near the transmembrane region is identical to the highly regulated cleavage site of the membrane-anchored transforming growth factor-alpha precursor.
8194490|The polypeptide of 653 amino acids has an overall identity of 72% with human and porcine endoglin. 
8194490|The transmembrane and cytoplasmic domains of all three proteins differ by two to four amino acids and are 70% identical to the corresponding regions of the TGF beta binding protein, betaglycan. 
1692830|Endoglin is a major glycoprotein of human vascular endothelium.
1692830|The N-terminal sequence of placental endoglin was determined and found within the deduced protein sequence, thus confirming the identity of the cDNA and revealing a partial signal peptide. 
1692830|Endoglin is a type I integral membrane protein of Mr = 68,051 with an extracellular region of 561 amino acids, a hydrophobic transmembrane domain, and a 47-residue cytoplasmic tail.
1692830|There are four potential N-linked glycosylation sites in the N-terminal domain and a probable O-glycan domain rich in Ser and Thr residues proximal to the membrane-spanning domain. 
1692830|The sequence contains an RGD tripeptide (374-376), the first identified on a surface protein of endothelium. 
7864874|Our previous study showed that porcine ZP1, one of the major glycoproteins of porcine zona pellucida, was divided into two components (porcine ZP4 and ZP2), and suggested it was a homologue of mouse ZP2.
7864874|The deduced amino acid sequence of porcine ZP1 shared a 54% and 63% identity with those of mouse and human ZP2, respectively. 
7841460|Within the ZPA, ZPB and ZPC gene families, the DNA and deduced amino acid sequences are highly homologous to each other, and are most homologous between members of the same order within the class mammalia.
VFUS_VACCC.struc:
2033392|Examination of the sequences revealed an open reading frame encoding a 10K peptide with significant amino acid homology to the 14K 'fusion' protein reported in vaccinia virus. 
1856205|An Mr 35,000 polypeptide, which bound antibody to the purified RNA polymerase, was synthesized in reticulocyte lysates programmed with viral mRNA that hybridized to a 2,300-base pair segment of the viral genome.
1856205|One open reading frame that could encode a 35,400-Da protein was identified as rpo35 on the basis of mRNA hybridization, cell-free translation, and immunoprecipitation.
1856205|The identification was confirmed by sequencing tryptic peptides of the authentic Mr 35,000 RNA polymerase subunit. 
1856205|Antiserum to the purified recombinant protein, expressed in bacteria, reacted specifically with a Mr 35,000 polypeptide that was detected starting 2 h after virus infection and that co-sedimented with RNA polymerase purified from virions.
2822962|A library of rabbit poxvirus DNA fragments contained in the expression cloning vector lambda gt11 was screened with monoclonal antibodies that react specifically against a 14-kilodalton envelope protein of vaccinia virus and rabbit poxvirus. 
2822962|The 14-kilodalton protein appears to play an important role in virus penetration at the level of cell fusion; it also elicits neutralizing antibodies, and it forms covalently linked trimers on the surface of virions and in infected cells (Rodriguez et al., J. Virol. 56:482-488, 1985; Rodriguez et al., J. Virol. 61:395-404, 1987). 
2822962|Restriction enzyme analysis and hybridization studies mapped the 14-kilodalton encoding sequences in the middle of vaccinia virus HindIII A DNA fragment. 
2822962|The sequence spans 330 nucleotides and codes for a protein with a molecular weight of 12,500 and an isoelectric point of 6.3. 
2822962|There are two small hydrophobic regions, one at the C terminus (11 amino acids) and the other at the N terminus (5 amino acids).
2822962|The protein contains two cysteines for oligomer formation and one glycosylation site. 
2822962|Inspection of the deduced amino acid sequence of the 14-kilodalton protein revealed consensus sites with the hemagglutinin precursor of influenza A virus and with adenylate kinase and cytochrome c of various species.
2389560|We have identified the virus-induced fusion protein as a 14-kDa envelope protein, based on the ability of a 14-kDa specific monoclonal antibody (mAbC3) to block vaccinia virus-induced fusion-from-within and fusion-from-without.
2389560|We provide genetic evidence for a role of the 14-kDa protein in cell fusion, since insertion of the 14-kDa encoding gene into the genome of nonfusogenic mutant viruses generates heterozygous viruses that now acquire acid pH-dependent fusion activity. 
2389560|DNA sequence analyses of the 14-kDa encoding gene of the mutant viruses, 65-16 and 101-14, reveal N-terminal deletions of 46 and 10 amino acids, respectively.
2389560|These deletions remove a small hydrophobic region at the N-terminus of the 14-kDa protein and prevent fusion. 
2389560|Our findings demonstrate that vaccinia virus can induce strong fusion of cells in culture at acid pH implying some entry of the virus by endocytosis, that the 14-kDa virus envelope protein is the fusogenic protein, and that the N-terminal proximal region is involved in fusion.
VGLG_IHNV.struc:
2741347|The deduced amino acid sequence of G shows that the encoded protein is a typical transmembrane glycoprotein of 524 amino acids containing a cleavable amino-terminal signal peptide, two potential N-linked glycosylation sites, a hydrophobic membrane anchor domain near the carboxy terminus, and a cytoplasmic domain at the carboxy terminus. 
2741347|Somewhat unusual is the appearance of two charged amino acid residues, aspartate and arginine, within the putative membrane anchor sequence. 
2741347|Expression of the G gene in COS cells resulted in production of a glycosylated protein of mol wt 71,000 which was recognized by anti-Chandipura antibodies.
2741347|Like the viral G protein, the expressed G contained covalently linked palmitic acid. 
2741347|However, unlike its vesicular stomatitis virus (Indiana serotype) counterpart, the Chandipura G protein has no potential palmitate-accepting cysteine residue within its cytoplasmic domain. 
2741347|Thus, the covalent attachment of fatty acid to this molecule may occur at one or both of the cysteines within the membrane anchor domain. 
1413521|The first ORF encodes a polypeptide comprising 623 residues which was identified by peptide sequencing as the virion G protein. 
1413521|The deduced amino acid sequence of the G protein includes putative signal and transmembrane domains and five potential glycosylation sites. 
1413521|The second ORF encodes a polypeptide of 586 amino acids which also has characteristics of a rhabdovirus glycoprotein, including putative signal and transmembrane domains and eight potential glycosylation sites, and appears to correspond to a 90-kDa nonstructural glycoprotein (GNS) identified in BEFV-infected cells (Walker et al. [1991] J. Gen. Virol. 72, 67-74).
1413521|A database search indicated that both the G and GNS proteins share significant amino acid sequence homology with other rhabdovirus G proteins and with each other. 
1413521|Highest homology scores for each protein were with sigma virus and vesicular stomatitis virus serotypes.
3459163|Evidence for the existence of a remnant protein gene in the 423 nucleotide long G-L intergenic region is presented.
6268840|The G protein mRNA is 1,665 nucleotides long, excluding polyadenylic acid, and encodes a protein of 511 amino acids including a signal peptide of 16 amino acids. 
6268840|G protein contains two large hydrophobic domains, one in the signal peptide and the other in the transmembrane segment near the COOH terminus. 
6268840|Two sites of glycosylation are predicted at amino acid residues 178 and 335. 
6268840|The mRNA encoding the vesicular stomatitis virus M protein is 831 nucleotides long, excluding polyadenylic acid, and encodes a protein of 229 amino acids. 
6268840|The predicted M protein sequence does not contain any long hydrophobic or nonpolar domains that might promote membrane association. 
6268840|The protein is rich in basic amino acids and contains a highly basic amino terminal domain. 
6298453|The mRNA is 1,573 nucleotides long (excluding polyadenylic acid) and encodes a protein of 517 amino acids.
6298453|An amino acid identity of 50.9% was found for the two VSV serotypes.
6298453|Approximately 20% identity was found between the rabies virus and VSV New Jersey glycoproteins.
6298453|The positions and sizes of the transmembrane domains, the signal sequences, and the glycosylation sites are identical in both VSV serotypes. 
6298453|Two of five serine residues which were possible esterification sites for palmitate in the glycoprotein from the Indiana serotype are changed to glycine residues in the glycoprotein from the New Jersey serotype. 
6298453|Because the glycoprotein of the New Jersey serotype does not contain esterified palmitate, we suggest that one or both of these residues are the probable esterification sites in the glycoprotein from the Indiana serotype.
2139267|Deduced protein sequences are highly similar to those of the pathogenic PV strain, homologies ranging from 90.6% for the M to 98.6% for the L protein. 
1954257|Although the protein encoded by this ORF displayed no similarity with other rhabdovirus proteins, it was supposed that the cDNA had been reverse-transcribed from a readthrough mRNA encoding successively for the M2 and the G proteins.
3033264|The G-protein cDNA is 1,609 nucleotides long (excluding the polyadenylic acid) and encodes a protein of 508 amino acids.
3033264|An amino acid identity of approximately 20% was found between infectious hematopoietic necrosis virus and the two vesicular stomatitis virus serotypes and between infectious hematopoietic necrosis virus and rabies virus. 
3033264|The positions and sizes of the signal sequence and transmembrane domain and the possible glycosylation sites were determined.
1736537|Compared with that of the prototype strain CVS, this sequence displayed 10% divergence in overall amino acid composition. 
1736537|However only 6% divergence was noted in the ectodomain suggesting that structural constraints are exerted on this portion of the glycoprotein.
1736537|A human strain isolated on cell culture from the saliva of a patient with clinical rabies had only five amino acid differences with the canine isolate, an indication of their close relatedness.
1736537|One of them concerned antigenic site III where arginine at position 333 was replaced by glutamine.