creators_name: Luthra-Guptasarma, Manni
creators_name: Singh, Balvinder
type: article
datestamp: 2012-02-14 12:16:00
lastmod: 2012-02-14 12:16:00
metadata_visibility: show
title: HLA-B27 lacking associated beta2-microglobulin rearranges to auto-display or cross-display residues 169-181: a novel molecular mechanism for spondyloarthropathies.
ispublished: pub
subjects: QR
full_text_status: restricted
keywords: HLA-B27; Ankylosing spondylitis; Protein misfolding; Detailed molecular mechanism; MHC auto display; Autoimmune disorders
note: Copyright of this article belongs to Elsevier Science.
abstract: Expression of the MHC class I allele, HLA-B27, is correlated with autoimmune disease. The misfolding and association of B27 heavy chains through non-native disulfide bonds has recently been implicated. Here, we propose that beta2m-free, peptide-free heavy chains support a helix-coil transition in the segment leading from the alpha2 domain to the alpha3 domain, facilitating rotation of backbone angles around residues 167/168, and allowing residues 169-181 (identical to a known B27 ligand) to loop around and occupy the molecule's own peptide-binding cleft. Such 'auto-display', occurring either within B27 molecules, or between B27 molecules, could provoke autoimmune attack.
date: 2004-09-24
date_type: published
publication: FEBS letters
volume: 575
number: 1-3
publisher: Elsevier Science
pagerange: 1-8
refereed: TRUE
issn: 0014-5793
official_url: http://www.sciencedirect.com/science/article/pii/S0014579304010385
related_url_url: http://www.sciencedirect.com/science/article/pii/S0014579304010385
related_url_type: pub
citation:   Luthra-Guptasarma, Manni and Singh, Balvinder  (2004) HLA-B27 lacking associated beta2-microglobulin rearranges to auto-display or cross-display residues 169-181: a novel molecular mechanism for spondyloarthropathies.  FEBS letters, 575 (1-3).  pp. 1-8.  ISSN 0014-5793     
document_url: http://crdd.osdd.net/open/970/1/balwinder2004.pdf