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2rrm

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Revision as of 22:05, 5 August 2016

Interplay between phosphatidyl-inositol-phosphates and claudins upon binding to the 1st PDZ domain of zonula occludens 1

Structural highlights

2rrm is a 1 chain structure with sequence from Lk3 transgenic mice. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ZO1_MOUSE] 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 (By similarity).

Publication Abstract from PubMed

Zonula occludens-1 (ZO-1) is a scaffolding molecule critical to the formation of intercellular adhesion structures, such as tight junctions (TJs) and adherens junctions (AJs). ZO-1 contains three PDZ domains followed by a GUK domain and a ZU5 domain. The first PDZ of ZO-1 (ZO-1(PDZ1)) serves as a protein-protein interaction module and interacts with the C-termini of almost all claudins to initiate the formation of a belt-like structure on the lateral membranes, thereby promoting TJ formation. It has been recently reported that approximately 15% of all PDZ domains bind phosphoinositides, and ZO-1(PDZ1) is the one of these. Here we report the (15)N, (13)C, and (1)H chemical shift assignments of the first PDZ domain of mouse ZO-1. The resonance assignments obtained in this work may contribute in clarifying the interplay between the two binary interactions, ZO-1(PDZ1)-claudins and ZO-1(PDZ1)-phospholipids, and suggesting a novel regulation mechanism underlying the formation and maintenance of cell-cell adhesion machinery downstream of the phospholipid signaling pathways.

(1)H, (13)C, and (15)N resonance assignment of the first PDZ domain of mouse ZO-1.,Umetsu Y, Goda N, Taniguchi R, Satomura K, Ikegami T, Furuse M, Hiroaki H Biomol NMR Assign. 2011 Mar 24. PMID:21431884^[1]

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

References

↑ Umetsu Y, Goda N, Taniguchi R, Satomura K, Ikegami T, Furuse M, Hiroaki H. (1)H, (13)C, and (15)N resonance assignment of the first PDZ domain of mouse ZO-1. Biomol NMR Assign. 2011 Mar 24. PMID:21431884 doi:10.1007/s12104-011-9301-x

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Interplay between phosphatidyl-inositol-phosphates and claudins upon binding to the 1st PDZ domain of zonula occludens 1==
 <StructureSection load='2rrm' size='340' side='right' caption='[[2rrm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rrm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RRM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rrm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RRM 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=2rrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rrm RCSB], [http://www.ebi.ac.uk/pdbsum/2rrm 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=2rrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrm OCA], [http://pdbe.org/2rrm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rrm RCSB], [http://www.ebi.ac.uk/pdbsum/2rrm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrm ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2rrm" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Mus musculus]]
+[[Category: Lk3 transgenic mice]]
 [[Category: Furuse, M]]
 [[Category: Goda, N]]

2rrm

From Proteopedia

Revision as of 22:05, 5 August 2016

Interplay between phosphatidyl-inositol-phosphates and claudins upon binding to the 1st PDZ domain of zonula occludens 1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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