Elliott W L, Stille C J, Thomas L J, Humphreys R E
J Immunol. 1987 May 1;138(9):2949-52.
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.
当我们研究这样一个假说，即从外来抗原消化而来的两亲性α螺旋肽与II类主要组织相容性复合体（MHC）分子的外来抗原结合位点（表位）结合，以便呈递给T细胞受体时，我们在Ii中发现了这样一个延伸的两亲性螺旋。据推测，这个两亲性螺旋会将Ii与II类MHC抗原结合，直到在含有消化后的外来抗原的内体中释放。然后这些两亲性Ii多肽可能会聚合，从而不与外来抗原竞争与II类MHC分子的结合。各种结构模型与这些观点一致，并导致了对特定形式的聚合相互作用的推测。
