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Toxins 2010, 2(10), 2411-2427; doi:10.3390/toxins2102411

ADAM-15 Disintegrin-Like Domain Structure and Function

Thrombosis Research Institute, Manresa Road, London, SW3 6LR, UK
Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SA, UK
Author to whom correspondence should be addressed.
Received: 30 August 2010 / Revised: 13 October 2010 / Accepted: 18 October 2010 / Published: 19 October 2010
(This article belongs to the Special Issue Disintegrins: Structure-Function and Translational Potential)
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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.
Keywords: ADAM protein; Snake venom toxin; disintegrin; integrin; RGD-motif ADAM protein; Snake venom toxin; disintegrin; integrin; RGD-motif
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Lu, D.; Scully, M.; Kakkar, V.; Lu, X. ADAM-15 Disintegrin-Like Domain Structure and Function. Toxins 2010, 2, 2411-2427.

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