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| Rádis-Baptista,G.; Moreno,F. B. M. B.; Nogueira,L. L.; Martins,A. M. C.; Toyama,D. O.; Toyama,M. H.; Azevedo Jr,W. F.; Cavada,B. S.; Yamane,T.. |
| Snake venom (sv) C-type lectins encompass a group of hemorrhagic toxins, which are able to interfere with hemostasis. They share significant similarity in their primary structures with C-type lectins of other animals, and also present a conserved carbohydrate recognition domain (CRD). A very well studied sv C-type lectin is the heterodimeric toxin, convulxin (CVX), from the venoms of South American rattlesnakes, Crotalus durissus terrificus and C. d. cascavella. It consists of two subunits, alfa (CVXalpha , 13.9 kDa) and beta (CVXbeta , 12.6 kDa), joined by inter and intra-chain disulfide bounds, and is arranged in a tetrameric alpha4beta4 conformation. Convulxin is able to activate platelet and induce their aggregation by acting via p62/GPVI collagen... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Crotalus durisssus venom; Snake venom C-type lectin; Homology modeling; Platelet aggregation; Antimicrobial activity. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992005000400013 |
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