The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core

J Biol Chem. 1980 Apr 10;255(7):2652-5.

Abstract

The three-dimensional structures of the snake venom postsynaptic neurotoxins and of the domains in wheat germ agglutinin show a remarkably similar overall folding pattern, consisting of equivalently placed, but variably sized loops which are held together by four similarly positioned disulfide bonds. Furthermore, occurrence of this wheat germ agglutinin-neurotoxin domain fold is predicted not only in the snake venom cardiotoxins and cytotoxins with neurotoxin-matched half-cystine sequence positions, but also for two small plant proteins, hevein and ragweed pollen allergen Ra5, on the basis of a nearly exact match of their half-cystine, sequence positions with those of the wheat germ agglutinin domain.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Disulfides*
  • Elapid Venoms*
  • Erabutoxins*
  • Lectins*
  • Neurotoxins*
  • Plant Lectins
  • Pollen
  • Protein Binding
  • Protein Conformation
  • Wheat Germ Agglutinins

Substances

  • Disulfides
  • Elapid Venoms
  • Lectins
  • Neurotoxins
  • Plant Lectins
  • Wheat Germ Agglutinins
  • Erabutoxins