HLA-B27 lacking associated beta2-microglobulin rearranges to auto-display or cross-display residues 169-181: a novel molecular mechanism for spondyloarthropathies.
DIR@IMTECH: CSIR-Institute of Microbial Technology
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Title |
HLA-B27 lacking associated beta2-microglobulin rearranges to auto-display or cross-display residues 169-181: a novel molecular mechanism for spondyloarthropathies.
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Creator |
Luthra-Guptasarma, Manni
Singh, Balvinder |
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Subject |
QR Microbiology
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Description |
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.
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Publisher |
Elsevier Science
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Date |
2004-09-24
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Identifier |
http://crdd.osdd.net/open/970/1/balwinder2004.pdf
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 |
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Relation |
http://www.sciencedirect.com/science/article/pii/S0014579304010385
http://crdd.osdd.net/open/970/ |
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