{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T09:23:54Z","timestamp":1791278634780,"version":"4.1.0"},"reference-count":101,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2010,10,19]],"date-time":"2010-10-19T00:00:00Z","timestamp":1287446400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>The ADAM (a disintegrin-like and metalloproteinase) proteins are a family of transmembrane cell-surface proteins with important functions in adhesion and proteolytic processing in all animals. Human ADAM-15 is the only member of the ADAM family with the integrin binding motif Arg-Gly-Asp (RGD) in its disintegrin-like domain. This motif is also found in most snake venom disintegrins and other disintegrin-like proteins. This unique RGD motif within ADAM-15 serves as an integrin ligand binding site, through which it plays a pivotal role in interacting with integrin receptors, a large family of heterodimeric transmembrane glycoproteins. This manuscript will present a review of the RGD-containing disintegrin-like domain structures and the structural features responsible for their activity as antagonists of integrin function in relation to the canonical RGD template.<\/jats:p>","DOI":"10.3390\/toxins2102411","type":"journal-article","created":{"date-parts":[[2010,10,19]],"date-time":"2010-10-19T11:51:56Z","timestamp":1287489116000},"page":"2411-2427","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["ADAM-15 Disintegrin-Like Domain Structure and Function"],"prefix":"10.3390","volume":"2","author":[{"given":"Dong","family":"Lu","sequence":"first","affiliation":[{"name":"Thrombosis Research Institute, Manresa Road, London, SW3 6LR, UK"},{"name":"Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SA, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mike","family":"Scully","sequence":"additional","affiliation":[{"name":"Thrombosis Research Institute, Manresa Road, London, SW3 6LR, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vijay","family":"Kakkar","sequence":"additional","affiliation":[{"name":"Thrombosis Research Institute, Manresa Road, London, SW3 6LR, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinjie","family":"Lu","sequence":"additional","affiliation":[{"name":"Thrombosis Research Institute, Manresa Road, London, SW3 6LR, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2010,10,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"168","DOI":"10.3181\/00379727-195-43129B","article-title":"Disintegrins: a family of integrin inhibitory proteins from viper venoms","volume":"195","author":"Gould","year":"1990","journal-title":"Proc. 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