ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove.
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.
Antoniou
Antony N
AN
Cancer Sciences Division, University of Southampton School of Medicine, Southampton SO16 6YD, UK.
Santos
Susana G
SG
Campbell
Elaine C
EC
Lynch
Sarah
S
Arosa
Fernando A
FA
Powis
Simon J
SJ
D000818:Animals; D017124:Conserved Sequence; D003545:Cysteine / Q000737:chemistry*; D000949:Histocompatibility Antigens Class II / Q000737:chemistry*; D006801:Humans; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases / Q000378:metabolism*; D051381:Rats
D000949:Histocompatibility Antigens Class II; D010455:Peptides; D019704:Protein Disulfide-Isomerases; D003545:Cysteine