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

A.N Antoniou, S Santos, E.C Campbell, S Lynch, F.A Arosa, Simon John 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 alpha 3 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. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)1988-1892
Number of pages5
JournalFEBS Letters
Volume581
DOIs
Publication statusPublished - 15 May 2007

Keywords

  • immunology
  • major histocompatibility complex
  • ERp57
  • antigen presentation/processing
  • OXIDOREDUCTASE ERP57
  • LOADING COMPLEX
  • MOLECULES
  • CALRETICULIN
  • TAPASIN
  • TAP
  • TRANSPORTER
  • OPTIMIZATION
  • CHAPERONE
  • CALNEXIN

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