http://crdd.osdd.net/open/id/eprint/970 2012-02-14T12:16:00Z info:eu-repo/semantics/descriptiveMetadata HLA-B27 lacking associated beta2-microglobulin rearranges to auto-display or cross-display residues 169-181: a novel molecular mechanism for spondyloarthropathies. Luthra-Guptasarma, Manni Singh, Balvinder QR Microbiology 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. Elsevier Science 2004-09-24 Article PeerReviewed application/pdf http://crdd.osdd.net/open/970/1/balwinder2004.pdf http://www.sciencedirect.com/science/article/pii/S0014579304010385 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 http://crdd.osdd.net/open/970/ info:eu-repo/semantics/objectFile info:eu-repo/semantics/humanStartPage