4oep

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==Crystal structure of the ZO-1 PDZ1 domain in complex with the 7-mer Claudin1 C-terminal tail==
==Crystal structure of the ZO-1 PDZ1 domain in complex with the 7-mer Claudin1 C-terminal tail==
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<StructureSection load='4oep' size='340' side='right' caption='[[4oep]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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<StructureSection load='4oep' size='340' side='right'caption='[[4oep]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4oep]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OEP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4oep]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OEP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oeo|4oeo]], [[4oeq|4oeq]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<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=4oep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oep RCSB], [http://www.ebi.ac.uk/pdbsum/4oep PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4oep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oep OCA], [https://pdbe.org/4oep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oep RCSB], [https://www.ebi.ac.uk/pdbsum/4oep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oep ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ZO1_HUMAN 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.<ref>PMID:21240187</ref>
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[https://www.uniprot.org/uniprot/ZO1_HUMAN 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.<ref>PMID:21240187</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The molecular seal between epithelial cells, called the tight junction (TJ), is built by several membrane proteins, with claudins playing the most prominent role. The scaffold proteins of the zonula occludens (ZO) family are required for the correct localization of claudins, and hence formation of the TJ. The intracellular C-terminus of claudins binds to the N-terminal PDZ domain of ZO proteins (PDZ1). Of the 23 identified human claudin proteins, nine possess a tyrosine at the -6 position. Here we show that the claudin affinity for PDZ1 is dependent on the presence or absence of this tyrosine, and that the affinity is reduced if the tyrosine is modified by phosphorylation. The PDZ1 beta2-beta3 loop undergoes a significant conformational change to accommodate this tyrosine. Cell culture experiments support a regulatory role for this tyrosine. Plasticity has been recognized as a critical property of TJs that allow cell remodeling and migration. Our work provides a molecular framework for how TJ plasticity may be regulated.
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Structural basis of a key factor regulating the affinity between the zonula occludens first PDZ domain and claudins.,Nomme J, Antanasijevic A, Caffrey M, Van Itallie CM, Anderson JM, Fanning AS, Lavie A J Biol Chem. 2015 May 28. pii: jbc.M115.646695. PMID:26023235<ref>PMID:26023235</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lavie, A]]
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[[Category: Homo sapiens]]
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[[Category: Nomme, J]]
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[[Category: Large Structures]]
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[[Category: Cell adhesion]]
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[[Category: Lavie A]]
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[[Category: Claudin]]
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[[Category: Nomme J]]
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[[Category: Maguk]]
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[[Category: Pdz1]]
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[[Category: Scaffolding]]
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[[Category: Tight junction assembly]]
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Current revision

Crystal structure of the ZO-1 PDZ1 domain in complex with the 7-mer Claudin1 C-terminal tail

PDB ID 4oep

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