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Expression, purification and assembly of soluble multimeric MHC class II–invariant chain complexes
Author(s) -
Majera Dušana,
Kristan Katarina Črnigoj,
Neefjes Jacques,
Turk Dušan,
Mihelič Marko
Publication year - 2012
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/j.febslet.2012.03.038
Subject(s) - cd74 , mhc class ii , trimer , major histocompatibility complex , endosome , chemistry , mhc class i , transporter associated with antigen processing , mhc restriction , transmembrane domain , transmembrane protein , microbiology and biotechnology , biochemistry , biology , gene , dimer , receptor , organic chemistry
Major histocompatibility class (MHC) II molecules are essential for running adaptive immune response. They are produced in the ER and targeted to late endosomes with the help of invariant chain (Ii) trimers. Ii trimerization may be induced by the Ii TM domain. To enable mechanistic and structural studies of MHC class II–Ii assembly, soluble forms of the complexes were expressed. We show that Ii trimerizes in the absence of the transmembrane part, prior to binding of α/β chains. The biochemical analysis supports the suggestion that the MHC class II–Ii complexes are not necessarily trimers of trimers, but that the Ii trimer can also be occupied by one or two MHC class II complexes.