An hypothesis on the binding of an amphipathic, alpha helical sequence in Ii to the desetope of class II antigens
Biochemistry & Molecular Pharmacology
Graduate School of Biomedical Sciences; Department of Pharmacology; Department of Medicine
Medical Subject Headings
Animals; Histocompatibility Antigens Class II; Oligopeptides; Protein Conformation; Solubility; Structure-Activity Relationship; T-Lymphocytes
Life Sciences | Medicine and Health Sciences
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.
Rights and Permissions
Citation: J Immunol. 1987 May 1;138(9):2949-52
Journal of immunology (Baltimore, Md. : 1950)
Elliot, William L.; Stille, Christopher J.; Thomas, Lawrence James; and Humphreys, Robert E., "An hypothesis on the binding of an amphipathic, alpha helical sequence in Ii to the desetope of class II antigens" (1987). GSBS Student Publications. 341.