RT Journal Article
SR Electronic
T1 An hypothesis on the binding of an amphipathic, alpha helical sequence in Ii to the desetope of class II antigens.
JF The Journal of Immunology
JO J. Immunol.
FD American Association of Immunologists
SP 2949
OP 2952
VO 138
IS 9
A1 Elliott, W L
A1 Stille, C J
A1 Thomas, L J
A1 Humphreys, R E
YR 1987
UL http://www.jimmunol.org/content/138/9/2949.abstract
AB 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.