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The protein has two extra cysteine residues (XIII and XVI) that form an additional disulfide bond that is characteristically found in the disintegrin\u2010like domains of cellular metalloproteinases (ADAMs) and PIII snake venom Zn\u2010metalloproteinases (SVMPs). The C\u2010terminal cysteine\u2010rich domain of catrocollastatin\u2010C contains five disulfide bonds between nearest\u2010neighbor cysteines and a long range disulfide bridge between CysV and CysX. These results provide structural evidence for a redefinition of the disintegrin\u2010like and cysteine\u2010rich domain boundaries. An evolutionary pathway for ADAMs, PIII, and PII SVMPs based on disulfide bond engineering is also proposed.<\/jats:p>","DOI":"10.1110\/ps.9.7.1365","type":"journal-article","created":{"date-parts":[[2009,2,17]],"date-time":"2009-02-17T23:05:20Z","timestamp":1234911920000},"page":"1365-1373","source":"Crossref","is-referenced-by-count":29,"title":["The disulfide bond pattern of catrocollastatin C, a disintegrin\u2010like\/cysteine\u2010rich protein isolated from <i>Crotalus atrox<\/i> venom"],"prefix":"10.1002","volume":"9","author":[{"given":"Juan J.","family":"Calvete","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. 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