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Toxins 2011, 3(8), 991-1003; doi:10.3390/toxins3080991

Molecular Analysis of the Interaction of the Snake Venom Rhodocytin with the Platelet Receptor CLEC-2

1 Department of Biochemistry, University of Cambridge/ 80 Tennis Court Road, Cambridge, CB2 1GA, UK 2 Henry Wellcome Building for Molecular Physiology, University of Oxford/ Roosevelt Drive, Oxford, OX3 7BN, UK
* Author to whom correspondence should be addressed.
Received: 6 July 2011 / Revised: 21 July 2011 / Accepted: 8 August 2011 / Published: 10 August 2011
(This article belongs to the Special Issue Snake Venoms)
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The Malayan pit viper, Calloselasma rhodostoma, produces a potent venom toxin, rhodocytin (aggretin) which causes platelet aggregation. Rhodocytin is a ligand for the receptor CLEC-2 on the surface of platelets. The interaction of these two molecules initiates a signaling pathway which results in platelet activation and aggregation. We have previously solved the crystal structures of CLEC-2 and of rhodocytin, and have proposed models by which tetrameric rhodocytin may interact with either two monomers of CLEC-2, or with one or two copies of dimeric CLEC-2. In the current study we use a range of approaches to analyze the molecular interfaces and dynamics involved in the models of the interaction of rhodocytin with either one or two copies of dimeric CLEC-2, and their implications for clustering of CLEC-2 on the platelet surface.
Keywords: rhodocytin; CLEC-2; platelets; thrombosis rhodocytin; CLEC-2; platelets; thrombosis
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Watson, A.A.; O’Callaghan, C.A. Molecular Analysis of the Interaction of the Snake Venom Rhodocytin with the Platelet Receptor CLEC-2. Toxins 2011, 3, 991-1003.

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