3e17
From Proteopedia
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| - | + | ==Crystal structure of the second PDZ domain from human Zona Occludens-2== | |
| - | + | <StructureSection load='3e17' size='340' side='right' caption='[[3e17]], [[Resolution|resolution]] 1.75Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3e17]] is a 2 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=3E17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E17 FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TJP2, X104, ZO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | [[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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e17 RCSB], [http://www.ebi.ac.uk/pdbsum/3e17 PDBsum]</span></td></tr> |
| - | + | </table> | |
| - | ==Function== | + | == Disease == |
| + | [[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> | ||
| + | == 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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/3e17_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human zonula occludens 2 (ZO-2) protein is a multi-domain protein that consists of an SH3 domain, a GK domain and three copies of a PDZ domain with slight divergence. The three PDZ domains act as protein-recognition modules that may mediate protein assembly and subunit localization. The crystal structure of the second PDZ domain of ZO-2 (ZO-2 PDZ2) was determined by molecular replacement at 1.75 A resolution, revealing a dimer in the asymmetric unit. The dimer is stabilized by extensive symmetrical domain-swapping of the beta1 and beta2 strands. Structural comparison shows that the ZO-2 PDZ2 homodimer may have a similar ligand-binding pattern to the ZO-1 PDZ2-connexin 43 complex. | ||
| - | + | Structure of the second PDZ domain from human zonula occludens 2.,Chen H, Tong S, Li X, Wu J, Zhu Z, Niu L, Teng M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt, 4):327-30. Epub 2009 Mar 25. PMID:19342771<ref>PMID:19342771</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Chen, H | + | [[Category: Chen, H]] |
| - | [[Category: Niu, L W | + | [[Category: Niu, L W]] |
| - | [[Category: Teng, M K | + | [[Category: Teng, M K]] |
| - | [[Category: Tong, S L | + | [[Category: Tong, S L]] |
[[Category: Alternative promoter usage]] | [[Category: Alternative promoter usage]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
Revision as of 14:26, 18 December 2014
Crystal structure of the second PDZ domain from human Zona Occludens-2
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