Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC

Nat Struct Mol Biol. 2007 Feb;14(2):169-71. doi: 10.1038/nsmb1193. Epub 2007 Jan 14.


'Superantigens' (SAgs) trigger the massive activation of T cells by simultaneous interactions with MHC and TCR receptors, leading to human diseases. Here we present the first crystal structure, at 2.5-A resolution, of a complete ternary complex between a SAg and its two receptors, HLA-DR1/HA and TCR. The most striking finding is that the SAg Mycoplasma arthritidis mitogen, unlike others, has direct contacts not only with TCR Vbeta but with TCR Valpha.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, Bacterial
  • Crystallography, X-Ray
  • HLA-DR1 Antigen / chemistry*
  • Hemagglutinins / chemistry*
  • Humans
  • Mice
  • Mitogens / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Mycoplasma arthritidis / immunology
  • Peptides / chemistry
  • Proteins / chemistry*
  • Receptors, Antigen, T-Cell, alpha-beta / chemistry*
  • Superantigens / chemistry*


  • Antigens, Bacterial
  • HLA-DR1 Antigen
  • Hemagglutinins
  • Mitogens
  • Mycoplasma arthritidis mitogen
  • Peptides
  • Proteins
  • Receptors, Antigen, T-Cell, alpha-beta
  • Superantigens

Associated data

  • PDB/2ICW