Chemistry of peptide interactions with MHC proteins

Curr Opin Immunol. 1992 Feb;4(1):79-86. doi: 10.1016/0952-7915(92)90130-7.

Abstract

X-ray crystallographic and peptide-MHC binding studies have begun to clarify the interaction between antigenic peptides and MHC proteins at the molecular level. At the same time, our understanding of the mechanisms of peptide-MHC interactions in physiologic cellular conditions has been significantly expanded by the isolation and characterization of naturally processed antigenic peptides.

Publication types

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

MeSH terms

  • Animals
  • Antigen-Presenting Cells / immunology
  • Antigen-Presenting Cells / metabolism
  • Antigens / immunology
  • Antigens / metabolism*
  • Binding Sites
  • Chemical Phenomena
  • Chemistry, Physical
  • HLA Antigens / chemistry
  • HLA Antigens / immunology
  • HLA Antigens / metabolism
  • HLA-B27 Antigen / metabolism
  • HLA-B27 Antigen / ultrastructure
  • Histocompatibility Antigens / chemistry
  • Histocompatibility Antigens / immunology
  • Histocompatibility Antigens / metabolism*
  • Histocompatibility Antigens Class II / immunology
  • Histocompatibility Antigens Class II / metabolism
  • Humans
  • Hydrogen-Ion Concentration
  • Mice
  • Models, Biological
  • Peptide Fragments / chemistry
  • Peptide Fragments / immunology
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / metabolism*
  • Phospholipids / metabolism
  • Protein Binding
  • Protein Conformation
  • X-Ray Diffraction

Substances

  • Antigens
  • HLA Antigens
  • HLA-B27 Antigen
  • Histocompatibility Antigens
  • Histocompatibility Antigens Class II
  • Peptide Fragments
  • Phospholipids