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2bfx

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[[Image:2bfx.gif|left|200px]]
 
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==Mechanism of Aurora-B activation by INCENP and inhibition by Hesperadin.==
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The line below this paragraph, containing "STRUCTURE_2bfx", creates the "Structure Box" on the page.
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<StructureSection load='2bfx' size='340' side='right'caption='[[2bfx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bfx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#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=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
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{{STRUCTURE_2bfx| PDB=2bfx | SCENE= }}
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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=2bfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfx OCA], [https://pdbe.org/2bfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfx RCSB], [https://www.ebi.ac.uk/pdbsum/2bfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AUKBA_XENLA AUKBA_XENLA] Serine/threonine-protein kinase 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. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Phosphorylates 'Ser-10' of histone H3 during mitosis.<ref>PMID:12221116</ref> <ref>PMID:11350965</ref> <ref>PMID:17199039</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bfx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2bfx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Aurora family serine/threonine kinases control mitotic progression, and their deregulation is implicated in tumorigenesis. Aurora A and Aurora B, the best-characterized members of mammalian Aurora kinases, are approximately 60% identical but bind to unrelated activating subunits. The structure of the complex of Aurora A with the TPX2 activator has been reported previously. Here, we report the crystal structure of Aurora B in complex with the IN-box segment of the inner centromere protein (INCENP) activator and with the small molecule inhibitor Hesperadin. The Aurora B:INCENP complex is remarkably different from the Aurora A:TPX2 complex. INCENP forms a crown around the small lobe of Aurora B and induces the active conformation of the T loop allosterically. The structure represents an intermediate state of activation of Aurora B in which the Aurora B C-terminal segment stabilizes an open conformation of the catalytic cleft, and a critical ion pair in the kinase active site is impaired. Phosphorylation of two serines in the carboxyl terminus of INCENP generates the fully active kinase.
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'''MECHANISM OF AURORA-B ACTIVATION BY INCENP AND INHIBITION BY HESPERIDIN.'''
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Mechanism of Aurora B activation by INCENP and inhibition by hesperadin.,Sessa F, Mapelli M, Ciferri C, Tarricone C, Areces LB, Schneider TR, Stukenberg PT, Musacchio A Mol Cell. 2005 Apr 29;18(3):379-91. PMID:15866179<ref>PMID:15866179</ref>
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==Overview==
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Aurora family serine/threonine kinases control mitotic progression, and their deregulation is implicated in tumorigenesis. Aurora A and Aurora B, the best-characterized members of mammalian Aurora kinases, are approximately 60% identical but bind to unrelated activating subunits. The structure of the complex of Aurora A with the TPX2 activator has been reported previously. Here, we report the crystal structure of Aurora B in complex with the IN-box segment of the inner centromere protein (INCENP) activator and with the small molecule inhibitor Hesperadin. The Aurora B:INCENP complex is remarkably different from the Aurora A:TPX2 complex. INCENP forms a crown around the small lobe of Aurora B and induces the active conformation of the T loop allosterically. The structure represents an intermediate state of activation of Aurora B in which the Aurora B C-terminal segment stabilizes an open conformation of the catalytic cleft, and a critical ion pair in the kinase active site is impaired. Phosphorylation of two serines in the carboxyl terminus of INCENP generates the fully active kinase.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2BFX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFX OCA].
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</div>
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<div class="pdbe-citations 2bfx" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Mechanism of Aurora B activation by INCENP and inhibition by hesperadin., Sessa F, Mapelli M, Ciferri C, Tarricone C, Areces LB, Schneider TR, Stukenberg PT, Musacchio A, Mol Cell. 2005 Apr 29;18(3):379-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15866179 15866179]
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*[[Centromere protein 3D structure|Centromere protein 3D structure]]
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[[Category: Protein complex]]
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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: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Areces, L B.]]
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[[Category: Areces LB]]
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[[Category: Ciferri, C.]]
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[[Category: Ciferri C]]
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[[Category: Mapelli, M.]]
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[[Category: Mapelli M]]
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[[Category: Musacchio, A.]]
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[[Category: Musacchio A]]
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[[Category: Schneider, T R.]]
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[[Category: Schneider TR]]
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[[Category: Sessa, F.]]
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[[Category: Sessa F]]
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[[Category: Stukenberg, P T.]]
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[[Category: Stukenberg PT]]
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[[Category: Tarricone, C.]]
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[[Category: Tarricone C]]
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[[Category: Inhibition]]
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[[Category: Kinase]]
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[[Category: Mitosis]]
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[[Category: Transferase complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:14:10 2008''
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Current revision

Mechanism of Aurora-B activation by INCENP and inhibition by Hesperadin.

PDB ID 2bfx

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