4n40

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'''Unreleased structure'''
 
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The entry 4n40 is ON HOLD until Paper Publication
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==Crystal structure of human Epithelial cell-transforming sequence 2 protein==
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<StructureSection load='4n40' size='340' side='right'caption='[[4n40]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4n40]] is a 1 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=4N40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N40 FirstGlance]. <br>
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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]] 3.106&#8491;</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=MSE:SELENOMETHIONINE'>MSE</scene></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=4n40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n40 OCA], [https://pdbe.org/4n40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n40 RCSB], [https://www.ebi.ac.uk/pdbsum/4n40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n40 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ECT2_HUMAN ECT2_HUMAN] Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.<ref>PMID:10579713</ref> <ref>PMID:14645260</ref> <ref>PMID:15254234</ref> <ref>PMID:15545273</ref> <ref>PMID:15642749</ref> <ref>PMID:16103226</ref> <ref>PMID:16495035</ref> <ref>PMID:16236794</ref> <ref>PMID:16170345</ref> <ref>PMID:19129481</ref> <ref>PMID:19617897</ref> <ref>PMID:19468300</ref> <ref>PMID:21189248</ref> <ref>PMID:21373644</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Homo sapiens ECT2 is a cell cycle regulator that plays critical roles in cytokinesis. ECT2 activity is restrained during interphase via intra-molecular interactions that involve its N-terminal triple-BRCT-domain and its C-terminal DH-PH domain. At anaphase, this self-inhibitory mechanism is relieved by Plk1-phosphorylated CYK-4, which directly engages the ECT2 BRCT domain. To provide a structural perspective for this auto-inhibitory property, we solved the crystal structure of the ECT2 triple-BRCT-domain. In addition, we systematically analyzed the interaction between the ECT2 BRCT domains with phospho-peptides derived from its binding partner CYK-4, and have identified Ser164 as the major phospho-residue that links CYK-4 to the second ECT2 BRCT domain.
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Authors: Zou, Y., Shao, Z.H., Li, F.D., Gong, D., Wang, C., Gong, Q., Shi, Y.
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Crystal structure of triple-BRCT-domain of ECT2 and insights into the binding characteristics to CYK-4.,Zou Y, Shao Z, Peng J, Li F, Gong D, Wang C, Zuo X, Zhang Z, Wu J, Shi Y, Gong Q FEBS Lett. 2014 Aug 25;588(17):2911-20. doi: 10.1016/j.febslet.2014.07.019. Epub , 2014 Jul 25. PMID:25068414<ref>PMID:25068414</ref>
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Description: Crystal structure of human Epithelial cell-transforming sequence 2 protein
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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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<div class="pdbe-citations 4n40" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Gong D]]
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[[Category: Gong Q]]
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[[Category: Li FD]]
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[[Category: Shao ZH]]
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[[Category: Shi Y]]
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[[Category: Wang C]]
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[[Category: Zou Y]]

Current revision

Crystal structure of human Epithelial cell-transforming sequence 2 protein

PDB ID 4n40

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