Abstract:
: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 alpha3 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Antoniou AN,Santos SG,Campbell EC,Lynch S,Arosa FA,Powis SJdoi
10.1016/j.febslet.2007.04.034subject
Has Abstractpub_date
2007-05-15 00:00:00pages
1988-92issue
10eissn
0014-5793issn
1873-3468pii
S0014-5793(07)00418-8journal_volume
581pub_type
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