Characterization of two platelet aggregation inhibitor-like polypeptides from viper venom
Two polypeptides, eristocophins I and II, have been characterized from leaf-nosed viper ( Eristocophis macmahoni) venom. They contain 10 half-Cys residues of a total of 61 62 residues, have 72% residue identity, and exhibit similarities to platelet aggregation inhibitors and segments of adhesive pro...
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| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1992-11, Vol.13 (6), p.1033-1037 |
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| creator | Siddiqi, Abdur Rehman Persson, Bengt Zaidi, Zafar H. Jörnvall, Hans |
| description | Two polypeptides, eristocophins I and II, have been characterized from leaf-nosed viper (
Eristocophis macmahoni) venom. They contain 10 half-Cys residues of a total of
61
62
residues, have 72% residue identity, and exhibit similarities to platelet aggregation inhibitors and segments of adhesive proteins. Eristocophin I contains the sequence Arg-Gly-Asp, known to inhibit fibrinogen interaction with the platelet receptor. Eristocophin II has Met instead of Arg in this sequence, and an adjacent Trp-Asn-Asp segment. The latter is also typical of adhesive proteins, thus linking two potentially functional segments in one molecule. Exchanges are maximal in these segments, suggesting that the polypeptides exhibit functional divergence with isoform differences in important regions. |
| doi_str_mv | 10.1016/0196-9781(92)90002-K |
| format | Article |
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Eristocophis macmahoni) venom. They contain 10 half-Cys residues of a total of
61
62
residues, have 72% residue identity, and exhibit similarities to platelet aggregation inhibitors and segments of adhesive proteins. Eristocophin I contains the sequence Arg-Gly-Asp, known to inhibit fibrinogen interaction with the platelet receptor. Eristocophin II has Met instead of Arg in this sequence, and an adjacent Trp-Asn-Asp segment. The latter is also typical of adhesive proteins, thus linking two potentially functional segments in one molecule. Exchanges are maximal in these segments, suggesting that the polypeptides exhibit functional divergence with isoform differences in important regions.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/0196-9781(92)90002-K</identifier><identifier>PMID: 1494485</identifier><identifier>CODEN: PPTDD5</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Adhesive proteins ; aggregation ; Amino Acid Sequence ; Aminoacids, peptides. Hormones. Neuropeptides ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; characterization ; Eristocophin ; Eristocophis macmahoni ; Fundamental and applied biological sciences. Psychology ; Homology ; inhibitors ; Isoforms ; Molecular Sequence Data ; Platelet Aggregation Inhibitors - analysis ; platelets ; Proteins ; RGD segment ; Sequence Alignment ; Sequence Homology, Amino Acid ; venom ; Venom peptides ; Viper venom ; Viper Venoms - analysis ; Viper Venoms - chemistry ; WND segment</subject><ispartof>Peptides (New York, N.Y. : 1980), 1992-11, Vol.13 (6), p.1033-1037</ispartof><rights>1992</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c332t-5b7471f30bf12032695bc911bcca6fbb8ee023b722edb52ca3f0ff16e34d3cc33</citedby><cites>FETCH-LOGICAL-c332t-5b7471f30bf12032695bc911bcca6fbb8ee023b722edb52ca3f0ff16e34d3cc33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/019697819290002K$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4490093$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1494485$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Siddiqi, Abdur Rehman</creatorcontrib><creatorcontrib>Persson, Bengt</creatorcontrib><creatorcontrib>Zaidi, Zafar H.</creatorcontrib><creatorcontrib>Jörnvall, Hans</creatorcontrib><title>Characterization of two platelet aggregation inhibitor-like polypeptides from viper venom</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>Two polypeptides, eristocophins I and II, have been characterized from leaf-nosed viper (
Eristocophis macmahoni) venom. They contain 10 half-Cys residues of a total of
61
62
residues, have 72% residue identity, and exhibit similarities to platelet aggregation inhibitors and segments of adhesive proteins. Eristocophin I contains the sequence Arg-Gly-Asp, known to inhibit fibrinogen interaction with the platelet receptor. Eristocophin II has Met instead of Arg in this sequence, and an adjacent Trp-Asn-Asp segment. The latter is also typical of adhesive proteins, thus linking two potentially functional segments in one molecule. Exchanges are maximal in these segments, suggesting that the polypeptides exhibit functional divergence with isoform differences in important regions.</description><subject>Adhesive proteins</subject><subject>aggregation</subject><subject>Amino Acid Sequence</subject><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>characterization</subject><subject>Eristocophin</subject><subject>Eristocophis macmahoni</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Homology</subject><subject>inhibitors</subject><subject>Isoforms</subject><subject>Molecular Sequence Data</subject><subject>Platelet Aggregation Inhibitors - analysis</subject><subject>platelets</subject><subject>Proteins</subject><subject>RGD segment</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>venom</subject><subject>Venom peptides</subject><subject>Viper venom</subject><subject>Viper Venoms - analysis</subject><subject>Viper Venoms - chemistry</subject><subject>WND segment</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtP3DAURi1ERYfHP6BSFqiCRYpfeXiDhEY8KpDYwIKVZTvXgyGJg-2Ziv76ZsgIdnTlxXfup-tzETok-BfBpDzFRJS5qGpyLOiJwBjT_GYLzUhdsbwgpdhGsw_kO9qN8XlkOBf1DtohXHBeFzP0OH9SQZkEwf1Vyfk-8zZLf3w2tCpBCylTi0WAxZS5_slpl3zIW_cC2eDbtwGG5BqImQ2-y1ZugJCtoPfdPvpmVRvhYPPuoYfLi_v5dX57d_V7fn6bG8Zoygtd8YpYhrUlFDNaikIbQYg2RpVW6xoAU6YrSqHRBTWKWWwtKYHxhpmxYw_9nHqH4F-XEJPsXDTQtqoHv4yyYrwQnPL_gqTkdY1pPYJ8Ak3wMQawcgiuU-FNEizX6uXaq1x7lYLKd_XyZhz7self6g6az6HJ9ZgfbXIVjWptUL1x8QMbL4OxWP_nbMJglLZyEGQ0DnoDjQtgkmy8-3qPf1ZOoXc</recordid><startdate>199211</startdate><enddate>199211</enddate><creator>Siddiqi, Abdur Rehman</creator><creator>Persson, Bengt</creator><creator>Zaidi, Zafar H.</creator><creator>Jörnvall, Hans</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>199211</creationdate><title>Characterization of two platelet aggregation inhibitor-like polypeptides from viper venom</title><author>Siddiqi, Abdur Rehman ; Persson, Bengt ; Zaidi, Zafar H. ; Jörnvall, Hans</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c332t-5b7471f30bf12032695bc911bcca6fbb8ee023b722edb52ca3f0ff16e34d3cc33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Adhesive proteins</topic><topic>aggregation</topic><topic>Amino Acid Sequence</topic><topic>Aminoacids, peptides. 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Psychology</topic><topic>Homology</topic><topic>inhibitors</topic><topic>Isoforms</topic><topic>Molecular Sequence Data</topic><topic>Platelet Aggregation Inhibitors - analysis</topic><topic>platelets</topic><topic>Proteins</topic><topic>RGD segment</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>venom</topic><topic>Venom peptides</topic><topic>Viper venom</topic><topic>Viper Venoms - analysis</topic><topic>Viper Venoms - chemistry</topic><topic>WND segment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Siddiqi, Abdur Rehman</creatorcontrib><creatorcontrib>Persson, Bengt</creatorcontrib><creatorcontrib>Zaidi, Zafar H.</creatorcontrib><creatorcontrib>Jörnvall, Hans</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Siddiqi, Abdur Rehman</au><au>Persson, Bengt</au><au>Zaidi, Zafar H.</au><au>Jörnvall, Hans</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of two platelet aggregation inhibitor-like polypeptides from viper venom</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>1992-11</date><risdate>1992</risdate><volume>13</volume><issue>6</issue><spage>1033</spage><epage>1037</epage><pages>1033-1037</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><coden>PPTDD5</coden><abstract>Two polypeptides, eristocophins I and II, have been characterized from leaf-nosed viper (
Eristocophis macmahoni) venom. They contain 10 half-Cys residues of a total of
61
62
residues, have 72% residue identity, and exhibit similarities to platelet aggregation inhibitors and segments of adhesive proteins. Eristocophin I contains the sequence Arg-Gly-Asp, known to inhibit fibrinogen interaction with the platelet receptor. Eristocophin II has Met instead of Arg in this sequence, and an adjacent Trp-Asn-Asp segment. The latter is also typical of adhesive proteins, thus linking two potentially functional segments in one molecule. Exchanges are maximal in these segments, suggesting that the polypeptides exhibit functional divergence with isoform differences in important regions.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>1494485</pmid><doi>10.1016/0196-9781(92)90002-K</doi><tpages>5</tpages></addata></record> |
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| ispartof | Peptides (New York, N.Y. : 1980), 1992-11, Vol.13 (6), p.1033-1037 |
| issn | 0196-9781 1873-5169 |
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| subjects | Adhesive proteins aggregation Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Biological and medical sciences characterization Eristocophin Eristocophis macmahoni Fundamental and applied biological sciences. Psychology Homology inhibitors Isoforms Molecular Sequence Data Platelet Aggregation Inhibitors - analysis platelets Proteins RGD segment Sequence Alignment Sequence Homology, Amino Acid venom Venom peptides Viper venom Viper Venoms - analysis Viper Venoms - chemistry WND segment |
| title | Characterization of two platelet aggregation inhibitor-like polypeptides from viper venom |
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