Structure of the snake-venom toxin convulxin
Batuwangala, T., Leduc, M., Gibbins, J. M., Bon, C. and Jones, E. Y. (2004) Structure of the snake-venom toxin convulxin. Acta Crystallographica Section D- Biological Crystallography, 60 (1). pp. 46-53. ISSN 0907-4449
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To link to this article DOI: 10.1107/s0907444903021620
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 Angstrom 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.
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