Initial structural analysis of an alpha4beta4 C-type lectin from the venom of Crotalus durissus terrificus

Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1813-5. doi: 10.1107/s0907444903016202. Epub 2003 Sep 19.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crotalid Venoms / chemistry*
  • Crotalus
  • Crystallization
  • Crystallography, X-Ray
  • Disulfides / chemistry
  • Lectins, C-Type / chemistry*
  • Models, Molecular
  • Protein Structure, Quaternary
  • Protein Subunits

Substances

  • Crotalid Venoms
  • Disulfides
  • Lectins, C-Type
  • Protein Subunits
  • convulxin