title: A case for chaperones in antigen processing.
abstract: The assembly of peptide-MHC-class-II molecule complexes by antigen-presenting cells is far more efficient than would be predicted from studies of peptide binding to purified MHC class II molecules in vitro. One possible explanation for this discrepancy is that proteins in the antigen-presenting cell facilitate the assembly process. Here, Diane DeNagel and Susan Pierce present the case for involvement of members of the chaperone/heat shock protein 70 family in the intracellular assembly of processed-antigen-MHC-class-II-molecule complexes.
authors.affiliation: Dept of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500.
authors.forename: D C
authors.initials: DC
authors.lastname: DeNagel
authors.forename: S K
authors.initials: SK
authors.lastname: Pierce
mesh_terms: D000595:Amino Acid Sequence; D000938:Antigen-Presenting Cells / Q000276:immunology*; D006360:Heat-Shock Proteins / Q000276:immunology*; D000949:Histocompatibility Antigens Class II / Q000276:immunology; D008969:Molecular Sequence Data
chemical_list: D006360:Heat-Shock Proteins; D000949:Histocompatibility Antigens Class II