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ERp57 interacts with conserved cysteine residues in the MHC class I peptide‐binding groove
Author(s) -
Antoniou Antony N.,
Santos Susana G.,
Campbell Elaine C.,
Lynch Sarah,
Arosa Fernando A.,
Powis Simon J.
Publication year - 2007
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.2007.04.034
Subject(s) - cysteine , peptide , major histocompatibility complex , mhc class i , chemistry , mhc restriction , biochemistry , conserved sequence , mhc class ii , binding site , cd74 , peptide sequence , enzyme , gene
The oxidoreductase ERp57 is a component of the major histocompatibility complex (MHC) class I peptide‐loading complex. ERp57 can interact directly with MHC class I molecules, however, little is known about which of the cysteine residues within the MHC class I molecule are relevant to this interaction. MHC class I molecules possess conserved disulfide bonds between cysteines 101–164, and 203–259 in the peptide‐binding and α3 domain, respectively. By studying a series of mutants of these conserved residues, we demonstrate that ERp57 predominantly associates with cysteine residues in the peptide‐binding domain, thus indicating ERp57 has direct access to the peptide‐binding groove of MHC class I molecules during assembly.