Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

Acta Crystallogr D Biol Crystallogr

Publication Date

01/2004

Volume

60

Pages

46 - 53

Keywords

Amino Acid Sequence, Animals, Crotalid Venoms, Crotalus, Crystallography, X-Ray, Lectins, C-Type, Models, Molecular, Molecular Sequence Data, Platelet Membrane Glycoproteins, Sequence Alignment