Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1

Nature. 1993 Jul 1;364(6432):33-9. doi: 10.1038/364033a0.


The three-dimensional structure of the class II histocompatibility glycoprotein HLA-DR1 from human B-cell membranes has been determined by X-ray crystallography and is similar to that of class I HLA. Peptides are bound in an extended conformation that projects from both ends of an 'open-ended' antigen-binding groove. A prominent non-polar pocket into which an 'anchoring' peptide side chain fits is near one end of the binding groove. A dimer of the class II alpha beta heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA dimerization as a mechanism for initiating the cytoplasmic signalling events in T-cell activation.

Publication types

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

MeSH terms

  • B-Lymphocytes / immunology
  • Binding Sites
  • CD4 Antigens / metabolism
  • Cell Line
  • Computer Simulation
  • HLA-DR1 Antigen / chemistry*
  • HLA-DR1 Antigen / metabolism
  • Histocompatibility Antigens Class I / chemistry
  • Humans
  • Lymphocyte Activation
  • Models, Molecular
  • Peptides / metabolism
  • Protein Binding
  • Protein Conformation
  • Signal Transduction
  • T-Lymphocytes / immunology
  • X-Ray Diffraction


  • CD4 Antigens
  • HLA-DR1 Antigen
  • Histocompatibility Antigens Class I
  • Peptides