1gqm: Difference between revisions
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[[Image:1gqm.gif|left|200px]] | [[Image:1gqm.gif|left|200px]] | ||
'''THE STRUCTURE OF S100A12 IN A HEXAMERIC FORM''' | {{Structure | ||
|PDB= 1gqm |SIZE=350|CAPTION= <scene name='initialview01'>1gqm</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE STRUCTURE OF S100A12 IN A HEXAMERIC FORM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GQM is a [ | 1GQM is a [[Single protein]] structure of sequence 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=1GQM OCA]. | ||
==Reference== | ==Reference== | ||
The structure of S100A12 in a hexameric form and its proposed role in receptor signalling., Moroz OV, Antson AA, Dodson EJ, Burrell HJ, Grist SJ, Lloyd RM, Maitland NJ, Dodson GG, Wilson KS, Lukanidin E, Bronstein IB, Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):407-13. Epub 2002, Feb 21. PMID:[http:// | The structure of S100A12 in a hexameric form and its proposed role in receptor signalling., Moroz OV, Antson AA, Dodson EJ, Burrell HJ, Grist SJ, Lloyd RM, Maitland NJ, Dodson GG, Wilson KS, Lukanidin E, Bronstein IB, Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):407-13. Epub 2002, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11856825 11856825] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: s100a12]] | [[Category: s100a12]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:38 2008'' |
Revision as of 12:26, 20 March 2008
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, resolution 2.70Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
THE STRUCTURE OF S100A12 IN A HEXAMERIC FORM
OverviewOverview
S100A12 is a member of the S100 subfamily of EF-hand calcium-binding proteins; it has been shown to be one of the ligands of the 'receptor for advanced glycation end products' (RAGE) that belongs to the immunoglobulin superfamily and is involved in diabetes, Alzheimer's disease, inflammation and tumour invasion. The structure of the dimeric form of native S100A12 from human granulocytes in the presence of calcium in space group R3 has previously been reported. Here, the structure of a second crystal form in space group P2(1) (unit-cell parameters a = 53.9, b = 100.5, c = 112.7A, beta = 94.6 degrees) solved at 2.7A resolution by molecular replacement using the R3 structure as a search model is reported. Like most S100 proteins, S100A12 is a dimer. However, in the P2(1) crystal form dimers of S100A12 are arranged in a spherical hexameric assembly with an external diameter of about 55 A stabilized by calcium ions bound between adjacent dimers. The putative target-binding sites of S100A12 are located at the outer surface of the hexamer, making it possible for the hexamer to bind several targets. It is proposed that the S100A12 hexameric assembly might interact with three extracellular domains of the receptor, bringing them together into large trimeric assemblies.
About this StructureAbout this Structure
1GQM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The structure of S100A12 in a hexameric form and its proposed role in receptor signalling., Moroz OV, Antson AA, Dodson EJ, Burrell HJ, Grist SJ, Lloyd RM, Maitland NJ, Dodson GG, Wilson KS, Lukanidin E, Bronstein IB, Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):407-13. Epub 2002, Feb 21. PMID:11856825
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