2kdd: Difference between revisions

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-{{Seed}}
-[[Image:2kdd.png|left|200px]]
-<!--
+==Solution structure of the conserved C-terminal dimerization domain of Borealin==
-The line below this paragraph, containing "STRUCTURE_2kdd", creates the "Structure Box" on the page.
+<StructureSection load='2kdd' size='340' side='right'caption='[[2kdd]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2kdd]] is a 2 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=2KDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KDD FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=2kdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdd OCA], [https://pdbe.org/2kdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kdd RCSB], [https://www.ebi.ac.uk/pdbsum/2kdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdd ProSAT]</span></td></tr>
-{{STRUCTURE_2kdd|  PDB=2kdd  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BOREA_HUMAN BOREA_HUMAN] Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.<ref>PMID:15260989</ref> <ref>PMID:15249581</ref> <ref>PMID:16571674</ref> <ref>PMID:18243099</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/2kdd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2kdd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The chromosomal passenger complex (CPC) has been identified as a master regulator of mitosis. In particular, proper chromosome segregation and cytokinesis depend on the correct localization and function of the CPC. Within the complex, the kinase Aurora B associates with Incenp, Survivin and Borealin. The stoichiometry of the complex as well as a complete understanding of how these four components interact with each other remains to be elucidated. Here, we identify a new domain of Borealin. We determined its structure using NMR spectroscopy and discovered a novel dimerization motif. Interestingly, we found that substitutions at Borealin T230, recently identified as an Mps1 phosphorylation site, can modulate the dimerization state of Borealin. Mutation of this single residue to alanine or valine impairs Aurora B activity during mitosis and causes chromosome segregation defects. This study reveals that Mps1 regulates the CPC through a novel Borealin domain.
-===Solution structure of the conserved C-terminal dimerization domain of Borealin===
+Phosphorylation of a Borealin dimerization domain is required for proper chromosome segregation.,Bourhis E, Lingel A, Phung Q, Fairbrother WJ, Cochran AG Biochemistry. 2009 Jun 17. PMID:19530738<ref>PMID:19530738</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2kdd" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19530738}}, adds the Publication Abstract to the page
+*[[Borealin|Borealin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19530738 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19530738}}
+__TOC__
+</StructureSection>
-==About this Structure==
-KDD is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDD OCA].
-==Reference==
-<ref group="xtra">PMID:19530738</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Bourhis, E.]]
+[[Category: Large Structures]]
-[[Category: Cochran, A G.]]
+[[Category: Bourhis E]]
-[[Category: Fairbrother, W J.]]
+[[Category: Cochran AG]]
-[[Category: Lingel, A.]]
+[[Category: Fairbrother WJ]]
-[[Category: Cell cycle]]
+[[Category: Lingel A]]
-[[Category: Cell division]]
-[[Category: Centromere]]
-[[Category: Chromosomal protein]]
-[[Category: Cytoplasm]]
-[[Category: Mitosis]]
-[[Category: Nucleus]]
-[[Category: Phosphoprotein]]
-[[Category: Polymorphism]]
-[[Category: Protein dimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep  3 16:25:03 2009''