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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Drenth, J; Low, BW; Richardson, JS; Wright, CS

Published Date

  • April 10, 1980

Published In

Volume / Issue

  • 255 / 7

Start / End Page

  • 2652 - 2655

PubMed ID

  • 6892639

Pubmed Central ID

  • 6892639

International Standard Serial Number (ISSN)

  • 0021-9258

Language

  • eng

Conference Location

  • United States