title: The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core.
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.
mesh_terms: D001665:Binding Sites; D004220:Disulfides; D004546:Elapid Venoms; D004870:Erabutoxins; D037102:Lectins; D009498:Neurotoxins; D037121:Plant Lectins; D011058:Pollen; D011485:Protein Binding; D011487:Protein Conformation; D014909:Wheat Germ Agglutinins
chemical_list: D004220:Disulfides; D004546:Elapid Venoms; D037102:Lectins; D009498:Neurotoxins; D037121:Plant Lectins; D014909:Wheat Germ Agglutinins; D004870:Erabutoxins