{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T19:21:26Z","timestamp":1787253686625,"version":"build-2736575974"},"reference-count":33,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":2161,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2003,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Disintegrins represent a group of cysteine\u2010rich peptides occurring in<jats:italic>Crotalidae<\/jats:italic>and<jats:italic>Viperidae<\/jats:italic>snake venoms, and are potent antagonists of several integrin receptors. A novel disintegrin, obtustatin, was isolated from the venom of the<jats:italic>Vipera lebetina obtusa<\/jats:italic>viper, and represents the first potent and selective inhibitor of the binding of integrin \u03b1<jats:sub>1<\/jats:sub>\u03b2<jats:sub>1<\/jats:sub>to collagen IV. The primary structure of obtustatin contains 41 amino acids and is the shortest disintegrin described to date. Obtustatin shares the pattern of cysteines of other short disintegrins. However, in contrast to known short disintegrins, the integrin\u2010binding loop of obtustatin is two residues shorter and does not express the classical RGD sequence. Using synthetic peptides, a KTS motif was identified as the integrin\u2010binding sequence. A three\u2010dimensional model of obtustatin, built by homology\u2010modeling structure calculations using different templates and alignments, strongly indicates that the novel KTS motif may reside at the tip of a flexible loop.<\/jats:p>","DOI":"10.1110\/ps.0230203","type":"journal-article","created":{"date-parts":[[2003,1,21]],"date-time":"2003-01-21T20:48:06Z","timestamp":1043182086000},"page":"366-371","source":"Crossref","is-referenced-by-count":40,"title":["Amino acid sequence and homology modeling of obtustatin, a novel non\u2010RGD\u2010containing short disintegrin isolated from the venom of<i>Vipera lebetina obtusa<\/i>"],"prefix":"10.1002","volume":"12","author":[{"given":"M. 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