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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) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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