Three-dimensional structures of MHC class I-peptide complexes: implications for peptide recognition.
Over the last decade, the number of crystal structures of major histocompatibility complex (MHC) class I-peptide complexes has increased rapidly. These studies have provided unique and fascinating insights into the structural basis of MHC-peptide interactions and the specificity of peptide recognition by MHC class I molecules.
Persson
K
K
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Schneider
G
G
D000595:Amino Acid Sequence; D000818:Animals; D017951:Antigen Presentation; D001665:Binding Sites; D018360:Crystallography, X-Ray; D015395:Histocompatibility Antigens Class I / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D051379:Mice; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000276:immunology* / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry / Q000378:metabolism; D014867:Water / Q000737:chemistry
D015395:Histocompatibility Antigens Class I; D046911:Macromolecular Substances; D010455:Peptides; D011948:Receptors, Antigen, T-Cell; D014867:Water