ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove

Antony N Antoniou, Susana G Santos, Elaine C Campbell, Sarah Lynch, Fernando A Arosa, Simon J Powis

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1988-92
Number of pages5
JournalFEBS Letters
Volume581
Issue number10
DOIs
Publication statusPublished - 15 May 2007
Externally publishedYes

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