title: How MHC class II molecules work: peptide-dependent completion of protein folding.
abstract: It is now clear that peptides play a key role in stabilizing the structure of MHC class II molecules. Here, Scheherazade Sadegh-Nasseri and Ron Germain propose that newly synthesized MHC class II, and indeed class I, molecules behave like partially folded proteins, with peptides acting as a surrogate portion of the MHC polypeptide structure that is necessary for completion of conformational maturation.
authors.affiliation: Lymphocyte Biology Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.
authors.forename: S
authors.initials: S
authors.lastname: Sadegh-Nasseri
authors.forename: R N
authors.initials: RN
authors.lastname: Germain
mesh_terms: D000818:Animals; D000949:Histocompatibility Antigens Class II / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D016693:Receptors, Antigen, T-Cell, alpha-beta / Q000737:chemistry*; D013329:Structure-Activity Relationship
chemical_list: D000949:Histocompatibility Antigens Class II; D016693:Receptors, Antigen, T-Cell, alpha-beta