2rrm: Difference between revisions

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[[~~Image~~:2rrm.~~png|left|200px~~]]

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

== 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]. <br>

</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>

<tr><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>

<table>

== 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>

~~The line below this paragraph~~, ~~containing "STRUCTURE_2rrm"~~, ~~creates the "Structure Box" on the page.~~

~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)

or the ~~SCENE parameter (which sets the initial scene displayed when the page is loaded)~~,

~~or leave the SCENE parameter empty for the default display~~.

-->

~~{{STRUCTURE_2rrm| PDB=2rrm | SCENE= }}~~

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

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

~~<!--~~

~~The line below this paragraph, {{ABSTRACT_PUBMED_21431884}}, adds the Publication Abstract to~~ the ~~page~~

__TOC__

~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 21431884 is the PubMed ID number~~.

</StructureSection>

-->

~~{{ABSTRACT_PUBMED_21431884}}~~

~~==About this Structure==~~

~~[[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].~~

==~~Reference~~==

<~~ref group="xtra">PMID:021431884<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Mus musculus]]

[[Category: Furuse, M.]]

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@@ Line 1: / Line 1: @@
-[[Image:2rrm.png|left|200px]]
+==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]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
+<tr><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>
+<table>
+<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>
-The line below this paragraph, containing "STRUCTURE_2rrm", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_2rrm|  PDB=2rrm  |  SCENE=  }}
-===Interplay between phosphatidyl-inositol-phosphates and claudins upon binding to the 1st PDZ domain of zonula occludens 1===
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_21431884}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 21431884 is the PubMed ID number.
+</StructureSection>
--->
-{{ABSTRACT_PUBMED_21431884}}
-==About this Structure==
-[[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].
-==Reference==
-<ref group="xtra">PMID:021431884</ref><references group="xtra"/>
 [[Category: Mus musculus]]
 [[Category: Furuse, M.]]