1uos

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uos OCA], [http://www.ebi.ac.uk/pdbsum/1uos PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uos RCSB]</span>
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[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:13:15 2008''

Revision as of 21:13, 30 March 2008


PDB ID 1uos

Drag the structure with the mouse to rotate
, resolution 2.7Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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