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


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).

Download

Full text not available from this repository.

Description/Abstract

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.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1093/emboj/21.11.2655
ISSNs: 0261-4189 (print)
Related URLs:
Keywords: chaperone, endoplasmic reticulum, MHC class I, oxidoreductase ERp57, protein folding
Subjects: R Medicine > R Medicine (General)
ePrint ID: 26197
Date :
Date Event
2002Published
Date Deposited: 20 Apr 2006
Last Modified: 16 Apr 2017 22:34
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/26197

Actions (login required)

View Item View Item