Crystal structure of the platelet activator convulxin, a disulfide-linked alpha(4)beta(4) cyclic tetramer from the venom of Crotalus durissus terrificus
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Data
2003-10-17
Autores
Murakami, M. T.
Zela, S. P.
Gava, L. M.
Michelan-Duarte, S.
Cintra, ACO
Arni, R. K.
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Editor
Elsevier B.V.
Resumo
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 hinds to platelet glycoprotein GPVI. The structure of CVX has been solved at 2.4 Angstrom 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 Ca2+ and carbohydrate binding regions. (C) 2003 Elsevier B.V. All rights reserved.
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C-type lectin, platelet activation factor, snake venom, Crotalus durissus terrificus, Crystal structure, cyclic alpha(4)beta(4)heterotetramer
Como citar
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 310, n. 2, p. 478-482, 2003.