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2osg

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Revision as of 06:59, 22 August 2018

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

Structural highlights

2osg is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[ZO2_HUMAN] Defects in TJP2 are involved in familial hypercholanemia (FHCA) [MIM:607748]. FHCA is a disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.^[1]

Function

[ZO2_HUMAN] Plays a role in tight junctions and adherens junctions.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN. Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. PMID:12704386 doi:10.1038/ng1147
↑ Wu J, Yang Y, Zhang J, Ji P, Du W, Jiang P, Xie D, Huang H, Wu M, Zhang G, Wu J, Shi Y. Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins. J Biol Chem. 2007 Dec 7;282(49):35988-99. Epub 2007 Sep 25. PMID:17897942 doi:10.1074/jbc.M703826200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2osg"

@@ Line 1: / Line 1: @@
 ==Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2==
 <StructureSection load='2osg' size='340' side='right' caption='[[2osg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2osg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
-</td></tr><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=2osg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2osg OCA], [http://pdbe.org/2osg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2osg RCSB], [http://www.ebi.ac.uk/pdbsum/2osg PDBsum]</span></td></tr>
+</td></tr><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=2osg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2osg OCA], [http://pdbe.org/2osg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2osg RCSB], [http://www.ebi.ac.uk/pdbsum/2osg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2osg ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/os/2osg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/os/2osg_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].
+</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=2osg ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2osg

From Proteopedia

Revision as of 06:59, 22 August 2018

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

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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