This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1umr
From Proteopedia
|
CRYSTAL STRUCTURE OF THE PLATELET ACTIVATOR CONVULXIN, A DISULFIDE LINKED A4B4 CYCLIC TETRAMER FROM THE VENOM OF CROTALUS DURISSUS TERRIFICUS
Overview
Convulxin (CVX), a C-type lectin, isolated from the venom of the South, American rattlesnake Crotalus durissus terrificus, causes cardiovascular, and respiratory disturbances and is a potent platelet activator which, binds to platelet glycoprotein GPVI. The structure of CVX has been solved, at 2.4A resolution to a crystallographic residual of 18.6%, (R(free)=26.4%). CVX is a disulfide linked heterodimer consisting of, homologous alpha and beta chains. The heterodimers are additionally linked, by disulfide bridges to form cyclic alpha(4)beta(4)heterotetramers. These, domains exhibit significant homology to the carbohydrate-binding domains, of C-type lectins, to the factor IX-binding protein (IX-bp), and to, flavocetin-A (Fl-A) but sequence and structural differences are observed, in both the domains in the putative Ca(2+)and carbohydrate binding, regions.
About this Structure
1UMR is a Protein complex structure of sequences from Crotalus durissus terrificus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the platelet activator convulxin, a disulfide-linked alpha4beta4 cyclic tetramer from the venom of Crotalus durissus terrificus., Murakami MT, Zela SP, Gava LM, Michelan-Duarte S, Cintra AC, Arni RK, Biochem Biophys Res Commun. 2003 Oct 17;310(2):478-82. PMID:14521935
Page seeded by OCA on Wed Nov 21 04:15:05 2007
