2osg

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{{STRUCTURE_2osg| PDB=2osg | SCENE= }}
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==Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2==
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===Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2===
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<StructureSection load='2osg' size='340' side='right' caption='[[2osg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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{{ABSTRACT_PUBMED_17897942}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2osg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OSG FirstGlance]. <br>
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==Disease==
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2osg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2osg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2osg RCSB], [http://www.ebi.ac.uk/pdbsum/2osg PDBsum]</span></td></tr>
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[[http://www.uniprot.org/uniprot/ZO2_HUMAN ZO2_HUMAN]] Defects in TJP2 are involved in familial hypercholanemia (FHCA) [MIM:[http://omim.org/entry/607748 607748]]. FHCA is a disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.<ref>PMID:12704386</ref>
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<table>
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== Disease ==
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==Function==
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[[http://www.uniprot.org/uniprot/ZO2_HUMAN ZO2_HUMAN]] Defects in TJP2 are involved in familial hypercholanemia (FHCA) [MIM:[http://omim.org/entry/607748 607748]]. FHCA is a disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.<ref>PMID:12704386</ref>
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== Function ==
[[http://www.uniprot.org/uniprot/ZO2_HUMAN ZO2_HUMAN]] Plays a role in tight junctions and adherens junctions.
[[http://www.uniprot.org/uniprot/ZO2_HUMAN ZO2_HUMAN]] Plays a role in tight junctions and adherens junctions.
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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/os/2osg_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/chain_selection.php?pdb_ID=2ata 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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Zonula occludens proteins (ZOs), including ZO1/2/3, are tight junction-associated proteins. Each of them contains three PDZ domains. It has been demonstrated that ZO1 can form either homodimers or heterodimers with ZO2 or ZO3 through the second PDZ domain. However, the underlying structural basis is not well understood. In this study, the solution structure of the second PDZ domain of ZO2 (ZO2-PDZ2) was determined using NMR spectroscopy. The results revealed a novel dimerization mode for PDZ domains via three-dimensional domain swapping, which can be generalized to homodimers of ZO1-PDZ2 or ZO3-PDZ2 and heterodimers of ZO1-PDZ2/ZO2-PDZ2 or ZO1-PDZ2/ZO3-PDZ2 due to high conservation between PDZ2 domains in ZO proteins. Furthermore, GST pulldown experiments and immunoprecipitation studies demonstrated that interactions between ZO1-PDZ2 and ZO2-PDZ2 and their self-associations indeed exist both in vitro and in vivo. Chemical cross-linking and dynamic laser light scattering experiments revealed that both ZO1-PDZ2 and ZO2-PDZ2 can form oligomers in solution. This PDZ domain-mediated oligomerization of ZOs may provide a structural basis for the polymerization of claudins, namely the formation of tight junctions.
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==About this Structure==
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Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins.,Wu J, Yang Y, Zhang J, Ji P, Du W, Jiang P, Xie D, Huang H, Wu M, Zhang G, Wu J, Shi Y J Biol Chem. 2007 Dec 7;282(49):35988-99. Epub 2007 Sep 25. PMID:17897942<ref>PMID:17897942</ref>
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[[2osg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OSG OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:017897942</ref><references group="xtra"/><references/>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ji, P.]]
[[Category: Ji, P.]]

Revision as of 19:19, 30 September 2014

Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2

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