1odb

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[[Image:1odb.png|left|200px]]
 
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==THE CRYSTAL STRUCTURE OF HUMAN S100A12 - COPPER COMPLEX==
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The line below this paragraph, containing "STRUCTURE_1odb", creates the "Structure Box" on the page.
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<StructureSection load='1odb' size='340' side='right'caption='[[1odb]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1odb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODB FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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{{STRUCTURE_1odb| PDB=1odb | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1odb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odb OCA], [https://pdbe.org/1odb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odb RCSB], [https://www.ebi.ac.uk/pdbsum/1odb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/S10AC_HUMAN S10AC_HUMAN] S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its proinflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of proinflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites. Possesses filariacidal and filariastatic activity. Calcitermin possesses antifungal activity against C.albicans and is also active against E.coli and P.aeruginosa but not L.monocytogenes and S.aureus.<ref>PMID:11522286</ref> <ref>PMID:17208591</ref> <ref>PMID:18292089</ref> <ref>PMID:19386136</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/od/1odb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1odb ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins. Together with S100A8 and S100A9, it belongs to the calgranulin subfamily, i.e. it is mainly expressed in granulocytes, although there is an increasing body of evidence of expression in keratinocytes and psoriatic lesions. As well as being linked to inflammation, allergy and neuritogenesis, S100A12 is involved in host-parasite response, as are the other two calgranulins. Recent data suggest that the function of the S100-family proteins is modulated not only by calcium, but also by other metals such as zinc and copper. Previously, the structure of human S100A12 in low-calcium and high-calcium structural forms, crystallized in space groups R3 and P2(1), respectively, has been reported. Here, the structure of S100A12 in complex with copper (space group P2(1)2(1)2; unit-cell parameters a = 70.6, b = 119.0, c = 90.2 A) refined at 2.19 A resolution is reported. Comparison of anomalous difference electron-density maps calculated with data collected with radiation of wavelengths 1.37 and 1.65 A shows that each monomer binds a single copper ion. The copper binds at an equivalent site to that at which another S100 protein, S100A7, binds zinc. The results suggest that copper binding may be essential for the functional role of S100A12 and probably the other calgranulins in the early immune response.
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===THE CRYSTAL STRUCTURE OF HUMAN S100A12 - COPPER COMPLEX===
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Structure of the human S100A12-copper complex: implications for host-parasite defence.,Moroz OV, Antson AA, Grist SJ, Maitland NJ, Dodson GG, Wilson KS, Lukanidin E, Bronstein IB Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):859-67. Epub 2003, Apr 25. PMID:12777802<ref>PMID:12777802</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1odb" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12777802}}, adds the Publication Abstract to the page
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*[[S100 proteins 3D structures|S100 proteins 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12777802 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12777802}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1odb]] is a 6 chain structure with 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=1ODB OCA].
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==Reference==
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<ref group="xtra">PMID:12777802</ref><ref group="xtra">PMID:11134923</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Antson, A A.]]
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[[Category: Large Structures]]
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[[Category: Bronstein, I B.]]
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[[Category: Antson AA]]
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[[Category: Dodson, G G.]]
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[[Category: Bronstein IB]]
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[[Category: Grist, S J.]]
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[[Category: Dodson GG]]
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[[Category: Lukanidin, E M.]]
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[[Category: Grist SJ]]
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[[Category: Maitland, N J.]]
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[[Category: Lukanidin EM]]
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[[Category: Moroz, O V.]]
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[[Category: Maitland NJ]]
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[[Category: Wilson, K S.]]
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[[Category: Moroz OV]]
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[[Category: Calcium binding]]
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[[Category: Wilson KS]]
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[[Category: Calcium-binding protein]]
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[[Category: Ef-hand]]
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[[Category: Host-parasite response]]
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[[Category: Metal-binding protein]]
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[[Category: S100 protein]]
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[[Category: X-ray structure]]
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Current revision

THE CRYSTAL STRUCTURE OF HUMAN S100A12 - COPPER COMPLEX

PDB ID 1odb

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