In: The EMBO Journal, 3 (1984), Nr. 4. pp. 873-877.
The invariant (Ii) chain is a membrane-spanning glycoprotein found intracellularly associated with class II major histocompatibility complex (MHC) molecules. Using hybridselected translation and the Ii-specific monoclonal antibody In-1, we have isolated a cDNA clone (pli-5) coding for most of the Ii chain. Sequence analysis of this clone reveals an open reading frame encoding 169 amino acid residues. The protein is rich in methionine and contains two potential N-glycosylation sites. No stretch of uncharged amino acid residues, characteristic for a membrane-spanning segment, is found close to the COOH-terminal end. There is one, however, close to the NH2-terminal end. As it is known that -20 amino acid residues of Ii chain are exposed on the cytoplasmic side, we conclude that the Ii chain spans the membrane exposing the NH2 terminus on the cytoplasmic side and the COOH terminus on the luminal side.
|Journal or Publication Title:||The EMBO Journal|
|Date Deposited:||17. Jul 2008 15:23|
|Page Range:||pp. 873-877|
|Faculties / Institutes:||Service facilities > Center for Molecular Biology Heidelberg|
|Subjects:||570 Life sciences|
|Uncontrolled Keywords:||major histocompatibility complex , invariant chain , cDNA cloning , transmembrane proteins|
|Schriftenreihe ID:||Works by Bernhard Dobberstein|