Mouse invariant chain gamma exhibits structural homology to both polymorphic subunits of the alpha, beta-core complex of I-Ak antigens.
The 3 major constituents of the I-Ak subregion-associated complex alpha, beta and gamma were obtained from splenocytes in homogeneous form by differential isolation methods. alpha, beta and gamma were compared on the primary structural level by enzymatic fragmentation procedures and tryptic peptide map analysis of radiolabeled proteins. The data indicate that the invariant chain gamma exhibits extensive structural homology to the polymorphic beta-light and the alpha-heavy chain. Thus, although not being encoded within the MHC gamma appears to belong structurally to the MHC-encoded class II proteins.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D000949:Histocompatibility Antigens Class II / Q000032:analysis*; D046911:Macromolecular Substances; D051379:Mice; D008809:Mice, Inbred C3H; D014357:Trypsin / Q000378:metabolism
D000949:Histocompatibility Antigens Class II; D046911:Macromolecular Substances; D014357:Trypsin