Premium
Mouse invariant chain γ exhibits structural homology to both polymorphic subunits of the α,β‐core complex of I‐A k antigens
Author(s) -
Reske Konrad,
Zecher Reinhard,
Stenger Elisabeth
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80436-0
Subject(s) - homology (biology) , major histocompatibility complex , homogeneous , cd74 , antigen , chemistry , mhc class ii , protein primary structure , peptide , invariant (physics) , biology , microbiology and biotechnology , genetics , peptide sequence , biochemistry , amino acid , gene , physics , combinatorics , mathematics , mathematical physics
The 3 major constituents of the I‐A k subregion‐associated complex α, β and γ were obtained from splenocytes in homogeneous form by differential isolation methods. α, β and γ 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 γ exhibits extensive structural homology to the polymorphic β‐light and the α‐heavy chain. Thus, although not being encoded within the MHC γ appears to belong structurally to the MHC‐encoded class II proteins.