{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T07:40:59Z","timestamp":1762674059271},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1993,7,1]]},"abstract":"<jats:p>Integrin binding to proteins often involves recognition of domains containing the arginine-glycine-aspartate (RGD) motif. Different binding affinities and specificities of the integrin-ligand protein interactions involve additional protein domains. The n.m.r. structure of the snake-venom protein echistatin suggested that the C-terminal portion of the molecule might be important, in addition to the RGD domain, in binding to the integrin glycoprotein IIbIIIa (GPIIbIIIa) [Saudek, Atkinson and Pelton (1991) Biochem. 30, 7369-7372]. The synthetic C-terminal peptide, echistatin-(40-49), PRNPHKGPAT, (1) inhibited binding of GPIIbIIIa to immobilized echistatin (IC50 3-6 mM), but did not inhibit binding of GPIIbIIIa to immobilized fibrinogen (up to 5 mM peptide), (2) activated GPIIbIIIa binding to fibronectin and vitronectin, usual ligands for the activated integrin, (3) activated binding of GPIIbIIIa to collagen type I and type IV, proteins not usually regarded as ligands for the integrin, and (4) stimulated 125I-fibrinogen binding by human platelets. These findings argue for an interaction of this non-RGD domain in echistatin with GPIIbIIIa, leading to activation of the integrin and extension of the ligand specificity to include immobilized collagen.<\/jats:p>","DOI":"10.1042\/bj2930263","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:33:18Z","timestamp":1439242398000},"page":"263-267","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["An echistatin C-terminal peptide activates GPIIbIIIa binding to fibrinogen, fibronectin, vitronectin and collagen type I and type IV"],"prefix":"10.1042","volume":"293","author":[{"given":"P S","family":"Wright","sequence":"first","affiliation":[{"name":"Marion Merrell Dow Research Institute, Cincinnati, OH 45215-6300, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"V","family":"Saudek","sequence":"additional","affiliation":[{"name":"Marion Merrell Dow Research Institute, Cincinnati, OH 45215-6300, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T J","family":"Owen","sequence":"additional","affiliation":[{"name":"Marion Merrell Dow Research Institute, Cincinnati, OH 45215-6300, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S L","family":"Harbeson","sequence":"additional","affiliation":[{"name":"Marion Merrell Dow Research Institute, Cincinnati, OH 45215-6300, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A J","family":"Bitonti","sequence":"additional","affiliation":[{"name":"Marion Merrell Dow Research Institute, Cincinnati, OH 45215-6300, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/293\/1\/263\/611474\/bj2930263.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/293\/1\/263\/611474\/bj2930263.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T22:31:41Z","timestamp":1637706701000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/293\/1\/263\/30233\/An-echistatin-C-terminal-peptide-activates"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1993,7,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1993,7,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2930263","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1993,7,1]]}}}