title: ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove.
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.
authors.affiliation: Cancer Sciences Division, University of Southampton School of Medicine, Southampton SO16 6YD, UK.
authors.forename: Antony N
authors.initials: AN
authors.lastname: Antoniou
authors.forename: Susana G
authors.initials: SG
authors.lastname: Santos
authors.forename: Elaine C
authors.initials: EC
authors.lastname: Campbell
authors.forename: Sarah
authors.initials: S
authors.lastname: Lynch
authors.forename: Fernando A
authors.initials: FA
authors.lastname: Arosa
authors.forename: Simon J
authors.initials: SJ
authors.lastname: Powis
mesh_terms: 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
chemical_list: D000949:Histocompatibility Antigens Class II; D010455:Peptides; D019704:Protein Disulfide-Isomerases; D003545:Cysteine