The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation

Nature. 1991 Sep 26;353(6342):321-5. doi: 10.1038/353321a0.


X-ray crystallography reveals electron density in the antigen-binding site of HLA-B27 that is an interpretable image of nonameric peptides in a largely extended conformation. Clear density exists for the main chain and several side chains and is consistent with the sequence of 11 nonameric self-peptides eluted from HLA-B27. Pockets in the antigen-binding cleft bind four side chains and the amino and carboxyl termini of the peptide.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Electrons
  • HLA-B27 Antigen / chemistry*
  • HLA-B27 Antigen / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Oligopeptides / metabolism*
  • Protein Binding
  • Protein Conformation


  • HLA-B27 Antigen
  • Oligopeptides