1uxs

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[[Image:1uxs.gif|left|200px]]<br /><applet load="1uxs" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1uxs.gif|left|200px]]
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caption="1uxs, resolution 1.55&Aring;" />
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'''CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2)OF EPSTEIN-BARR VIRUS'''<br />
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{{Structure
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|PDB= 1uxs |SIZE=350|CAPTION= <scene name='initialview01'>1uxs</scene>, resolution 1.55&Aring;
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2)OF EPSTEIN-BARR VIRUS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UXS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UXS OCA].
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1UXS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UXS OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15537660 15537660]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15537660 15537660]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: mhc (major histocompatibility complex)]]
[[Category: mhc (major histocompatibility complex)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:38:14 2008''

Revision as of 12:38, 20 March 2008


PDB ID 1uxs

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, resolution 1.55Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2)OF EPSTEIN-BARR VIRUS


Contents

Overview

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 pVIPR (RRKWRRWHL, derived from vasoactive intestinal peptide type 1 receptor (residues 400-408)) is observed only when the peptides are presented by B(*)2705 because of a salt bridge between Arg(5) of both peptides and the subtype-specific heavy chain residue Asp(116). Combined with functional studies using pLMP2/pVIPR-cross-reactive cytotoxic T cell lines and clones, together with target cells presenting these peptides or a modified peptide analogue, our results reveal that a pathogen-derived peptide can exhibit major histocompatibility complex class I subtype-dependent, drastically distinct binding modes. Furthermore, the results demonstrate that molecular mimicry between pLMP2 and pVIPR in the HLA-B27 context is an allele-dependent property.

Disease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]

About this Structure

1UXS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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