2kxr
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kxr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXR FirstGlance]. <br> | <table><tr><td colspan='2'>[[2kxr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXR 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=2kxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxr OCA], [https://pdbe.org/2kxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxr RCSB], [https://www.ebi.ac.uk/pdbsum/2kxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxr ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxr OCA], [https://pdbe.org/2kxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxr RCSB], [https://www.ebi.ac.uk/pdbsum/2kxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | [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> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Zonula occludens (ZO)-1 is a multi-domain scaffold protein known to have critical roles in the establishment of cell-cell adhesions and the maintenance of stable tissue structures through the targeting, anchoring, and clustering of transmembrane adhesion molecules and cytoskeletal proteins. Here, we report that ZO-1 directly binds to MRCKbeta, a Cdc42 effector kinase that modulates cell protrusion and migration, at the leading edge of migrating cells. Structural studies reveal that the binding of a beta hairpin from GRINL1A converts ZO-1 ZU5 into a complete ZU5-fold. A similar interaction mode is likely to occur between ZO-1 ZU5 and MRCKbeta. The interaction between ZO-1 and MRCKbeta requires the kinase to be primed by Cdc42 due to the closed conformation of the kinase. Formation of the ZO-1/MRCKbeta complex enriches the kinase at the lamellae of migrating cells. Disruption of the ZO-1/MRCKbeta complex inhibits MRCKbeta-mediated cell migration. These results demonstrate that ZO-1, a classical scaffold protein with accepted roles in maintaining cell-cell adhesions in stable tissues, also has an active role in cell migration during processes such as tissue development and remodelling. | ||
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| - | Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration.,Huo L, Wen W, Wang R, Kam C, Xia J, Feng W, Zhang M EMBO J. 2011 Feb 16;30(4):665-78. Epub 2011 Jan 14. PMID:21240187<ref>PMID:21240187</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2kxr" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
ZO1 ZU5 domain MC/AA mutation
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