1umr
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(New page: 200px<br /><applet load="1umr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1umr, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 02:07, 21 November 2007
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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
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