title: The wide diversity and complexity of peptides bound to class II MHC molecules.
abstract: The identification and quantitation of peptides selected by class II MHC molecules during natural processing of proteins is of key importance in understanding the repertoire and distribution of T cells. The examination of peptides selected by class II MHC molecules has depended greatly on mass spectrometry, a powerful technique that identifies and sequences peptides in complex mixtures with great sensitivity and precision. Such analysis has resulted in the identification of several factors, including the repertoire of peptides selected by MHC molecules during natural processing of proteins, motifs important for selection of processed peptides, conformational isomers of peptide-MHC complexes, and post-translational changes to the peptides.
authors.affiliation: Washington University School of Medicine, Department of Pathology and Immunology, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
authors.forename: Anish
authors.initials: A
authors.lastname: Suri
authors.forename: Scott B
authors.initials: SB
authors.lastname: Lovitch
authors.forename: Emil R
authors.initials: ER
authors.lastname: Unanue
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015496:CD4-Positive T-Lymphocytes / Q000276:immunology* / Q000378:metabolism; D000949:Histocompatibility Antigens Class II / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding / Q000276:immunology; D011499:Protein Processing, Post-Translational
chemical_list: D000949:Histocompatibility Antigens Class II; D010446:Peptide Fragments