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Snake Venom Disintegrins and Cell Migration
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ADAM-15 Disintegrin-Like Domain Structure and Function

by 1,2, 1, 1 and 1,*
1
Thrombosis Research Institute, Manresa Road, London, SW3 6LR, UK
2
Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SA, UK
*
Author to whom correspondence should be addressed.
Toxins 2010, 2(10), 2411-2427; https://doi.org/10.3390/toxins2102411
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)
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. View Full-Text
Keywords: ADAM protein; Snake venom toxin; disintegrin; integrin; RGD-motif ADAM protein; Snake venom toxin; disintegrin; integrin; RGD-motif
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MDPI and ACS Style

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

AMA Style

Lu D, Scully M, Kakkar V, Lu X. ADAM-15 Disintegrin-Like Domain Structure and Function. Toxins. 2010; 2(10):2411-2427.

Chicago/Turabian Style

Lu, Dong; Scully, Mike; Kakkar, Vijay; Lu, Xinjie. 2010. "ADAM-15 Disintegrin-Like Domain Structure and Function" Toxins 2, no. 10: 2411-2427.

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