1uos
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(New page: 200px<br /><applet load="1uos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uos, resolution 2.7Å" /> '''THE CRYSTAL STRUCTURE...)
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Revision as of 02:09, 21 November 2007
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THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN
Overview
Snake 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.
About this Structure
1UOS is a Protein complex structure of sequences from Crotalus durissus terrificus. Full crystallographic information is available from OCA.
Reference
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
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