The crystal structure of H-2Dd MHC class I complexed with the HIV-1-derived peptide P18-I10 at 2.4 A resolution: implications for T cell and NK cell recognition

Immunity. 1998 Aug;9(2):199-208. doi: 10.1016/s1074-7613(00)80602-0.

Abstract

The structure of H-2Dd complexed with the HIV-derived peptide P18-I10 (RGPGRAFVTI) has been determined by X-ray crystallography at 2.4 A resolution. This MHC class I molecule has an unusual binding motif with four anchor residues in the peptide (G2, P3, R/K/H5, and I/L/F9 or 10). The cleft architecture of H-2Dd includes a deep narrow passage accomodating the N-terminal part of the peptide, explaining the obligatory G2P3 anchor motif. Toward the C-terminal half of the peptide, p5R to p8V form a type I' reverse turn; residues p6A to p9T, and in particular p7F, are readily exposed. The structure is discussed in relation to functional data available for T cell and natural killer cell recognition of the H-2Dd molecule.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Epitopes / chemistry
  • H-2 Antigens / chemistry*
  • H-2 Antigens / metabolism
  • HIV Envelope Protein gp160 / chemistry*
  • Histocompatibility Antigen H-2D
  • Histocompatibility Antigens Class I / chemistry*
  • Histocompatibility Antigens Class I / metabolism
  • Killer Cells, Natural / immunology
  • Killer Cells, Natural / metabolism
  • Ligands
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Solvents
  • T-Lymphocytes / immunology

Substances

  • Epitopes
  • H-2 Antigens
  • HIV Envelope Protein gp160
  • Histocompatibility Antigen H-2D
  • Histocompatibility Antigens Class I
  • Ligands
  • Peptides
  • Solvents