The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection

Cell. 1994 Jan 14;76(1):39-50. doi: 10.1016/0092-8674(94)90171-6.

Abstract

Solution at 2.4 A resolution of the structure of H-2Db with the influenza virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides than can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Cloning, Molecular
  • Epitopes / chemistry*
  • H-2 Antigens / chemistry*
  • Histocompatibility Antigen H-2D
  • Hydrogen Bonding
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides
  • Polymerase Chain Reaction
  • Protein Conformation*
  • Protein Structure, Secondary*
  • Receptors, Antigen, T-Cell / metabolism
  • Recombinant Proteins / chemistry
  • X-Ray Diffraction / methods

Substances

  • Epitopes
  • H-2 Antigens
  • Histocompatibility Antigen H-2D
  • Oligodeoxyribonucleotides
  • Receptors, Antigen, T-Cell
  • Recombinant Proteins