Residues defining V beta specificity in staphylococcal enterotoxins

Nat Struct Biol. 1995 Aug;2(8):680-6. doi: 10.1038/nsb0895-680.

Abstract

The three-dimensional structure of staphylococcal enterotoxin C2 has been determined at 2.7 A resolution by x-ray diffraction, while the structures of enterotoxins A and E have been modelled based on their sequence homology to other staphylococcal enterotoxins. The T-cell receptor-binding sites of staphylococcal enterotoxin (SE) B and SEC2 are compared and the stereochemical interactions likely to be responsible for their differing V beta specificities are identified. A similar comparison is made between SEA and SEE.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray / methods
  • Enterotoxins / chemistry*
  • Enterotoxins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary*
  • Receptors, Antigen, T-Cell / metabolism
  • Sequence Homology, Amino Acid
  • Staphylococcus aureus

Substances

  • Enterotoxins
  • Receptors, Antigen, T-Cell
  • enterotoxin E, Staphylococcal
  • enterotoxin A, Staphylococcal
  • enterotoxin B, staphylococcal
  • enterotoxin C, staphylococcal