2rrm: Difference between revisions
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< | ==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]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rrm]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=2rrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrm OCA], [https://pdbe.org/2rrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrm RCSB], [https://www.ebi.ac.uk/pdbsum/2rrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrm ProSAT]</span></td></tr> | |||
-- | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ZO1_MOUSE 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). | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:21431884</ref> | |||
From MEDLINE®/PubMed®, 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: Large Structures]] | ||
== | |||
< | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Furuse | [[Category: Furuse M]] | ||
[[Category: Goda | [[Category: Goda N]] | ||
[[Category: Hiroaki | [[Category: Hiroaki H]] | ||
[[Category: Ikegami | [[Category: Ikegami T]] | ||
[[Category: Satomura | [[Category: Satomura K]] | ||
[[Category: Taniguchi | [[Category: Taniguchi R]] | ||
[[Category: Umetsu | [[Category: Umetsu Y]] | ||
Latest revision as of 10:03, 14 June 2023
Interplay between phosphatidyl-inositol-phosphates and claudins upon binding to the 1st PDZ domain of zonula occludens 1
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