Structure of the complex between human T-cell receptor, viral peptide and HLA-A2

Nature. 1996 Nov 14;384(6605):134-41. doi: 10.1038/384134a0.


Recognition by a T-cell antigen receptor (TCR) of peptide complexed with a major histocompatibility complex (MHC) molecule occurs through variable loops in the TCR structure which bury almost all the available peptide and a much larger area of the MHC molecule. The TCR fits diagonally across the MHC peptide-binding site in a surface feature common to all class I and class II MHC molecules, providing evidence that the nature of binding is general. A broadly applicable binding mode has implications for the mechanism of repertoire selection and the magnitude of alloreactions.

Publication types

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

MeSH terms

  • Crystallography, X-Ray
  • Gene Products, tax / chemistry*
  • Gene Products, tax / immunology
  • HLA-A2 Antigen / chemistry*
  • HLA-A2 Antigen / immunology
  • Human T-lymphotropic virus 1 / chemistry
  • Human T-lymphotropic virus 1 / immunology
  • Humans
  • Immune Tolerance
  • Immunoglobulin Fragments / chemistry
  • Major Histocompatibility Complex
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Receptors, Antigen, T-Cell / chemistry*
  • Receptors, Antigen, T-Cell / immunology
  • Signal Transduction


  • Gene Products, tax
  • HLA-A2 Antigen
  • Immunoglobulin Fragments
  • Receptors, Antigen, T-Cell