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