1uxw: Difference between revisions
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Revision as of 17:10, 30 October 2007
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CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2) OF EPSTEIN-BARR VIRUS
OverviewOverview
Molecular mimicry is discussed as a possible mechanism that may contribute, to the development of autoimmune diseases. It could also be involved in, the differential association of the human major histocompatibility, subtypes HLA-B(*)2705 and HLA-B(*)2709 with ankylosing spondylitis. These, two subtypes differ only in residue 116 of the heavy chain (Asp in, B(*)2705 and His in B(*)2709), but the reason for the differential disease, association is not understood. Using x-ray crystallography, we show here, that the viral peptide pLMP2 (RRRWRRLTV, derived from latent membrane, protein 2 (residues 236-244) of Epstein-Barr virus) is presented by the, B(*)2705 and B(*)2709 molecules in two drastically deviating, conformations. Extensive structural similarity between pLMP2 and the, self-peptide ... [(full description)]
About this StructureAbout this Structure
1UXW is a [Protein complex] structure of sequences from [Homo sapiens] with GOL as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Allele-dependent similarity between viral and self-peptide presentation by HLA-B27 subtypes., Fiorillo MT, Ruckert C, Hulsmeyer M, Sorrentino R, Saenger W, Ziegler A, Uchanska-Ziegler B, J Biol Chem. 2005 Jan 28;280(4):2962-71. Epub 2004 Nov 10. PMID:15537660
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