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4n40

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'''Unreleased structure'''
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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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N40 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<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=4n40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n40 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n40 RCSB], [http://www.ebi.ac.uk/pdbsum/4n40 PDBsum]</span></td></tr>
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<table>
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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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The entry 4n40 is ON HOLD until Paper Publication
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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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Authors: Zou, Y., Shao, Z.H., Li, F.D., Gong, D., Wang, C., Gong, Q., Shi, Y.
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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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Description: Crystal structure of human Epithelial cell-transforming sequence 2 protein
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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: Gong, D.]]
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[[Category: Gong, Q.]]
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[[Category: Li, F D.]]
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[[Category: Shao, Z H.]]
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[[Category: Shi, Y.]]
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[[Category: Wang, C.]]
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[[Category: Zou, Y.]]
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[[Category: Cell cycle]]
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[[Category: Triple brct domain]]

Revision as of 08:39, 27 August 2014

Crystal structure of human Epithelial cell-transforming sequence 2 protein

4n40, resolution 3.11Å

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