Initial structural analysis of an alpha(4)beta(4) C-type lectin from the venom of Crotalus durissus terrificus
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Blackwell Munksgaard
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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 Angstrom, and diffraction data were collected to 2.7 Angstrom. 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.
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Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 59, p. 1813-1815, 2003.
