An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501

Immunity. 1996 Mar;4(3):203-13. doi: 10.1016/s1074-7613(00)80429-x.


The crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket. The structure also reveals a novel conformation of the 8-mer peptide within the binding groove. The positions of the peptide N and C termini are nonstandard, but the classic pattern of hydrogen bonding to nonpolymorphic MHC class I residues is maintained, at the N terminus by addition of a water molecule, and at the C terminus by a substantial shift in the alpha 2 helix.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alleles*
  • Amino Acid Sequence
  • Base Sequence
  • Crystallography, X-Ray*
  • Gene Products, nef / chemistry
  • HLA-B35 Antigen / chemistry*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation


  • Gene Products, nef
  • HLA-B35 Antigen

Associated data