Initial structural analysis of an alpha4beta4 C-type lectin from the venom of Crotalus durissus terrificus.
Convulxin, an alphabeta C-type lectin, is a potent platelet activator isolated from the venom of the South American rattlesnake Crotalus durissus terrificus. It is a 26.5 kDa alphabeta heterodimer consisting of two homologous disulfide-linked chains. The crystals belong to space group I4, with unit-cell parameters a = b = 131.61, c = 121.85 A, and diffraction data were collected to 2.7 A. The structure was solved by molecular replacement and the asymmetric unit contains two alphabeta heterodimers, each of which forms a disulfide-linked cyclic alpha(4)beta(4) tetramer in the unit cell. These alpha(4)beta(4) tetramers are stacked to form a large solvent channel.
D000818:Animals; D003435:Crotalid Venoms / Q000737:chemistry*; D017839:Crotalus; D003460:Crystallization; D018360:Crystallography, X-Ray; D004220:Disulfides / Q000737:chemistry; D037181:Lectins, C-Type / Q000737:chemistry*; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D021122:Protein Subunits
D003435:Crotalid Venoms; D004220:Disulfides; D037181:Lectins, C-Type; D021122:Protein Subunits; C028890:convulxin