Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence

EMBO J. 2001 Jul 2;20(13):3306-12. doi: 10.1093/emboj/20.13.3306.

Abstract

The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 A resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S.aureus. SEH interacts with high affinity through a zinc ion with the beta1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cloning, Molecular
  • Crystallography, X-Ray / methods
  • Enterotoxins / chemistry*
  • Enterotoxins / immunology
  • HLA-DR1 Antigen / chemistry*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / immunology
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Staphylococcus aureus
  • Superantigens / chemistry
  • Superantigens / immunology
  • Zinc / chemistry
  • Zinc Fingers

Substances

  • Enterotoxins
  • HLA-DR1 Antigen
  • Recombinant Proteins
  • Staphylococcal enterotoxin H
  • Superantigens
  • Zinc

Associated data

  • PDB/1DLH
  • PDB/1ENF
  • PDB/1HXY