Crystal structure of staphylococcal enterotoxin B, a superantigen

Nature. 1992 Oct 29;359(6398):801-6. doi: 10.1038/359801a0.

Abstract

The three-dimensional structure of staphylococcal enterotoxin B, which is both a toxin and a super-antigen, has been determined to a resolution of 2.5 A. The unusual main-chain fold containing two domains may represent a general motif adopted by all staphylococcal enterotoxins. The T-cell receptor binding site encompasses a shallow cavity formed by both domains. The MHCII molecule binds to an adjacent site. Another cavity with possible biological activity was also identified.

Publication types

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

MeSH terms

  • Animals
  • Antigens, Bacterial / chemistry
  • Antigens, Bacterial / metabolism
  • Binding Sites
  • Enterotoxins / chemistry*
  • Enterotoxins / metabolism
  • Models, Molecular
  • Protein Conformation*
  • Protein Structure, Secondary*
  • Receptors, Antigen, T-Cell / metabolism
  • Staphylococcus aureus
  • X-Ray Diffraction

Substances

  • Antigens, Bacterial
  • Enterotoxins
  • Receptors, Antigen, T-Cell
  • enterotoxin B, staphylococcal