Molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2.

Journal article

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.

Authors: Watson, A; O'Callaghan, C

• Publication status: Published
• Journal: Toxins
• Volume: 3
• Issue: 8
• Pages: 991-1003
• Publication date: 2011-08-01
• DOI: 10.3390/toxins3080991
• EISSN: 2072-6651
• ISSN: 2072-6651
• Language: English
• Keywords: Ligands; Animals; Protein Conformation; Signal Transduction; Protein Binding; Platelet Aggregation; Algorithms; Lectins, C-Type; Agkistrodon; Viper Venoms; Blood Platelets