An hypothesis on the binding of an amphipathic, alpha helical sequence in Ii to the desetope of class II antigens.
When we investigated the hypothesis that amphipathic alpha helical peptides digested from foreign antigen bind to class II major histocompatability complex (MHC) molecules' binding site (desetope) for foreign antigen to be presented to T cell receptors, we found such an extended amphipathic helix in Ii. This amphipathic helix was hypothesized to bind Ii to class II MHC antigens until release in endosomes containing digested foreign antigen. Then these amphipathic Ii polypeptides might polymerize so as not to compete with foreign antigen for binding to class II MHC molecules. Various structural models were consistent with these views and led to the suggestion of specific forms of polymeric interaction.
D000818:Animals; D000949:Histocompatibility Antigens Class II / Q000276:immunology*; D009842:Oligopeptides / Q000276:immunology*; D011487:Protein Conformation; D012995:Solubility; D013329:Structure-Activity Relationship; D013601:T-Lymphocytes / Q000276:immunology*
D000949:Histocompatibility Antigens Class II; D009842:Oligopeptides