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2rcz

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Revision as of 10:55, 5 September 2018

Structure of the second PDZ domain of ZO-1

Structural highlights

2rcz is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	TJP1, ZO1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ZO1_HUMAN] The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells.^[1]

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

ZO-1 is a multidomain protein involved in cell-cell junctions and contains three PDZ domains, which are necessary for its function in vivo. PDZ domains play a central role in assembling diverse protein complexes through their ability to recognize short peptide motifs on other proteins. We determined the structure of the second of the three PDZ domains of ZO-1, which is known to promote dimerization as well as bind to C-terminal sequences on connexins. The dimer is stabilized by extensive symmetrical domain swapping of beta-strands, which is unlike any other known mechanism of PDZ dimerization. The canonical peptide-binding groove remains intact in both subunits of the PDZ2 dimer and is created by elements contributed from both monomers. This unique structure reveals an additional example of how PDZ domains dimerize and has multiple implications for both peptide binding and oligomerization in vivo.

Domain swapping within PDZ2 is responsible for dimerization of ZO proteins.,Fanning AS, Lye MF, Anderson JM, Lavie A J Biol Chem. 2007 Dec 28;282(52):37710-6. Epub 2007 Oct 9. PMID:17928286^[2]

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

References

↑ Huo L, Wen W, Wang R, Kam C, Xia J, Feng W, Zhang M. Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration. EMBO J. 2011 Feb 16;30(4):665-78. Epub 2011 Jan 14. PMID:21240187 doi:10.1038/emboj.2010.353
↑ Fanning AS, Lye MF, Anderson JM, Lavie A. Domain swapping within PDZ2 is responsible for dimerization of ZO proteins. J Biol Chem. 2007 Dec 28;282(52):37710-6. Epub 2007 Oct 9. PMID:17928286 doi:10.1074/jbc.M707255200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Structure of the second PDZ domain of ZO-1==
 <StructureSection load='2rcz' size='340' side='right' caption='[[2rcz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2rcz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RCZ FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TJP1, ZO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2rcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcz OCA], [http://pdbe.org/2rcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rcz RCSB], [http://www.ebi.ac.uk/pdbsum/2rcz PDBsum]</span></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=2rcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcz OCA], [http://pdbe.org/2rcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rcz RCSB], [http://www.ebi.ac.uk/pdbsum/2rcz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rcz ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/2rcz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/2rcz_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2rcz

From Proteopedia

Revision as of 10:55, 5 September 2018

Structure of the second PDZ domain of ZO-1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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