title: The complex route to MHC class I-peptide complexes.
abstract: The loading of peptides into the groove of MHC class I molecules prior to antigen presentation is a complex process. In this issue of Cell, Park et al. (2006) show that peptide loading gets a helping hand from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidoreductase activity.
authors.affiliation: Cancer Sciences Division, University of Southampton School of Medicine, Southampton SO16 6YD, UK. t.j.elliott@soton.ac.uk
authors.forename: Tim
authors.initials: T
authors.lastname: Elliott
authors.forename: Jacques
authors.initials: J
authors.lastname: Neefjes
mesh_terms: D017951:Antigen Presentation; D003586:Cytomegalovirus Infections / Q000276:immunology / Q000378:metabolism; D015395:Histocompatibility Antigens Class I / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D010084:Oxidation-Reduction; D010455:Peptides / Q000276:immunology / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D019704:Protein Disulfide-Isomerases / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000378:metabolism
chemical_list: D015395:Histocompatibility Antigens Class I; D010455:Peptides; D013438:Sulfhydryl Compounds; D046988:Proteasome Endopeptidase Complex; D019704:Protein Disulfide-Isomerases