1umr
From Proteopedia
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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 Thu Feb 21 15:26:12 2008
