1ymm

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[[Image:1ymm.gif|left|200px]]
[[Image:1ymm.gif|left|200px]]
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{{Structure
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|PDB= 1ymm |SIZE=350|CAPTION= <scene name='initialview01'>1ymm</scene>, resolution 3.500&Aring;
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The line below this paragraph, containing "STRUCTURE_1ymm", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= HLA-DRA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1ymm| PDB=1ymm | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ymm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ymm OCA], [http://www.ebi.ac.uk/pdbsum/1ymm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ymm RCSB]</span>
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'''TCR/HLA-DR2b/MBP-peptide complex'''
'''TCR/HLA-DR2b/MBP-peptide complex'''
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[[Category: Pyrdol, J.]]
[[Category: Pyrdol, J.]]
[[Category: Wucherpfennig, K W.]]
[[Category: Wucherpfennig, K W.]]
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[[Category: auto-immunity]]
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[[Category: Auto-immunity]]
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[[Category: protein-protein complex]]
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[[Category: Protein-protein complex]]
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[[Category: t cell repertoire]]
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[[Category: T cell repertoire]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:30:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:13:19 2008''
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Revision as of 13:30, 3 May 2008

Template:STRUCTURE 1ymm

TCR/HLA-DR2b/MBP-peptide complex


Overview

Autoimmune diseases are caused by self-reactive lymphocytes that have escaped deletion. Here we have determined the structure of the trimolecular complex for a T cell receptor (TCR) from a patient with multiple sclerosis that causes autoimmunity in transgenic mice. The structure showed a TCR topology notably different from that of antimicrobial TCRs. Rather than being centered on the peptide-major histocompatibility complex, this TCR contacted only the N-terminal peptide segment and made asymmetrical interactions with the major histocompatibility complex helices. The interaction was dominated by the hypervariable complementarity-determining region 3 loops, indicating that unconventional topologies are possible because of the unique complementarity-determining region 3 sequences created during rearrangement. This topology reduces the interaction surface with peptide and alters the geometry for CD4 association. We propose that unusual TCR-binding properties can permit autoreactive T cells to escape deletion.

About this Structure

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

Reference

Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor., Hahn M, Nicholson MJ, Pyrdol J, Wucherpfennig KW, Nat Immunol. 2005 May;6(5):490-6. Epub 2005 Apr 10. PMID:15821740 Page seeded by OCA on Sat May 3 16:30:49 2008

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