1umr
From Proteopedia
Crystal structure of the platelet activator convulxin, a disulfide linked a4b4 cyclic tetramer from the venom of Crotalus durissus terrificus
Structural highlights
FunctionSLA_CRODU Snake venom lectin that activates platelets by binding to the platelet collagen receptor glycoprotein VI (GP6) (PubMed:9153205). The indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3) also induced by the toxin is upstream the cytoskeletal translocation of GPIb, FcRgamma (FCER1G) and 14-3-3zeta (YWHAZ)(PubMed:16102113).[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedConvulxin (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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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