1py9: Difference between revisions
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|PDB= 1py9 |SIZE=350|CAPTION= <scene name='initialview01'>1py9</scene>, resolution 1.8Å | |PDB= 1py9 |SIZE=350|CAPTION= <scene name='initialview01'>1py9</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MOG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= MOG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1py9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1py9 OCA], [http://www.ebi.ac.uk/pdbsum/1py9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1py9 RCSB]</span> | |||
}} | }} | ||
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[[Category: Rossjohn, J.]] | [[Category: Rossjohn, J.]] | ||
[[Category: Tynan, F E.]] | [[Category: Tynan, F E.]] | ||
[[Category: anti-parallel dimer]] | [[Category: anti-parallel dimer]] | ||
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:06:11 2008'' | ||
Revision as of 23:06, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | |||||||
| Gene: | MOG (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of an autoantigen in multiple sclerosis
OverviewOverview
Myelin oligodendrocyte glycoprotein (MOG) is a key CNS-specific autoantigen for primary demyelination in multiple sclerosis. Although the disease-inducing role of MOG has been established, its precise function in the CNS remains obscure. To gain new insights into the physiological and immunopathological role of MOG, we determined the 1.8-A crystal structure of the MOG extracellular domain (MOGED). MOGED adopts a classical Ig (Ig variable domain) fold that was observed to form an antiparallel head-to-tail dimer. A dimeric form of native MOG was observed, and MOGED was also shown to dimerize in solution, consistent with the view of MOG acting as a homophilic adhesion receptor. The MOG35-55 peptide, a major encephalitogenic determinant recognized by both T cells and demyelinating autoantibodies, is partly occluded within the dimer interface. The structure of this key autoantigen suggests a relationship between the dimeric form of MOG within the myelin sheath and a breakdown of immunological tolerance to MOG that is observed in multiple sclerosis.
About this StructureAbout this Structure
1PY9 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis., Clements CS, Reid HH, Beddoe T, Tynan FE, Perugini MA, Johns TG, Bernard CC, Rossjohn J, Proc Natl Acad Sci U S A. 2003 Sep 16;100(19):11059-64. Epub 2003 Sep 5. PMID:12960396
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