MHC class II structure, occupancy and surface expression determined by post-endoplasmic reticulum antigen binding.
Class II major histocompatibility complex molecules undergo a change in structure upon stable binding of peptide antigen. Analysis of the site and extent of this change among class II molecules of splenic antigen-presenting cells reveals the preference of class II for peptide acquisition outside the endoplasmic reticulum and indicates that the class II presentation system is not saturated with self peptides. There are numerous empty class II molecules on the cell surface and peptide antigen is evidently important in regulating surface class II expression.
Germain
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Lymphocyte Biology Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.
Hendrix
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D000818:Animals; D000941:Antigens / Q000378:metabolism*; D001665:Binding Sites; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000378:metabolism; D002738:Chloroquine / Q000494:pharmacology; D004721:Endoplasmic Reticulum / Q000378:metabolism; D000949:Histocompatibility Antigens Class II / Q000737:chemistry* / Q000378:metabolism; D046911:Macromolecular Substances; D051379:Mice; D008815:Mice, Inbred Strains; D015394:Molecular Structure; D009113:Muramidase / Q000276:immunology; D010455:Peptides / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational / Q000187:drug effects
D000941:Antigens; D000949:Histocompatibility Antigens Class II; D046911:Macromolecular Substances; D010455:Peptides; D002738:Chloroquine; D009113:Muramidase