Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSnake venoms contain a number of proteins that interact with components of the haemostatic system that promote or inhibit events leading to blood-clot formation. The snake-venom protein convulxin (Cvx) binds glycoprotein (GP) VI, the platelet receptor for collagen, and triggers signal transduction. Here, the 2.7 A resolution crystal structure of Cvx is presented. In common with other members of this snake-venom protein family, Cvx is an alphabeta-heterodimer and conforms to the C-type lectin-fold topology. Comparison with other family members allows a set of Cvx residues that form a concave surface to be putatively implicated in GPVI binding. Unlike other family members, with the exception of flavocetin-A (FL-A), Cvx forms an (alphabeta)(4) tetramer. This oligomeric structure is consistent with Cvx clustering GPVI molecules on the surface of platelets and as a result promoting signal transduction activity. The Cvx structure and the location of the putative binding sites suggest a model for this multimeric signalling assembly. Structure of the snake-venom toxin convulxin.,Batuwangala T, Leduc M, Gibbins JM, Bon C, Jones EY Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):46-53. Epub 2003, Dec 18. PMID:14684891[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. ReferencesContents | ||||||||||||||||||
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