The University of Southampton
University of Southampton Institutional Repository

The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules

Record type: Article

The oxidoreductase ERp57 is an integral component of the peptide loading complex of major histocompatibility complex (MHC) class I molecules, formed during their chaperone-assisted assembly in the endoplasmic reticulum. Misfolded MHC class I molecules or those denied suitable peptides are retrotranslocated and degraded in the cytosol. The presence of ERp57 during class I assembly suggests it may be involved in the reduction of intrachain disulfides prior to retrotranslocation. We have studied the ability of ERp57 to reduce MHC class I molecules in vitro. Recombinant ERp57 specifically reduced partially folded MHC class I molecules, whereas it had little or no effect on folded and peptide-loaded MHC class I molecules. Reductase activity was associated with cysteines at positions 56 and 405 of ERp57, the N-terminal residues of the active CXXC motifs. Our data suggest that the reductase activity of ERp57 may be involved during the unfolding of MHC class I molecules, leading to targeting for degradation.

Full text not available from this repository.


Antoniou, Antony N., Ford, Stuart, Alphey, Magnus, Osborne, Andrew, Elliott, Tim and Powis, Simon J. (2002) The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules The EMBO Journal, 21, (11), pp. 2655-2663. (doi:10.1093/emboj/21.11.2655).

More information

Published date: 2002
Keywords: chaperone, endoplasmic reticulum, MHC class I, oxidoreductase ERp57, protein folding


Local EPrints ID: 26197
ISSN: 0261-4189
PURE UUID: 6a21ff87-174d-4491-afca-43471a61d961
ORCID for Tim Elliott: ORCID iD

Catalogue record

Date deposited: 20 Apr 2006
Last modified: 17 Jul 2017 16:08

Export record



Author: Antony N. Antoniou
Author: Stuart Ford
Author: Magnus Alphey
Author: Andrew Osborne
Author: Tim Elliott ORCID iD
Author: Simon J. Powis

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton:

ePrints Soton supports OAI 2.0 with a base URL of

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.