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2vrx

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{{Seed}}
 
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[[Image:2vrx.png|left|200px]]
 
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<!--
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==Structure of Aurora B kinase in complex with ZM447439==
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The line below this paragraph, containing "STRUCTURE_2vrx", creates the "Structure Box" on the page.
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<StructureSection load='2vrx' size='340' side='right'caption='[[2vrx]], [[Resolution|resolution]] 1.86&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'>[[2vrx]] 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=2VRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=447:N-(4-{[6-METHOXY-7-(3-MORPHOLIN-4-YLPROPOXY)QUINAZOLIN-4-YL]AMINO}PHENYL)BENZAMIDE'>447</scene></td></tr>
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-->
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
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{{STRUCTURE_2vrx| PDB=2vrx | SCENE= }}
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bfx|2bfx]], [[2vgo|2vgo]], [[2vgp|2vgp]], [[2bfy|2bfy]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=2vrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrx OCA], [https://pdbe.org/2vrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrx RCSB], [https://www.ebi.ac.uk/pdbsum/2vrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrx 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> [[https://www.uniprot.org/uniprot/INCEA_XENLA INCEA_XENLA]] 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. Probably acts through association with aurkb or aurkc. Seems to bind directly to microtubules.<ref>PMID:12221116</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/vr/2vrx_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=2vrx 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 kinases have emerged as potential targets in cancer therapy, and several drugs are currently undergoing preclinical and clinical validation. Whether clinical resistance to these drugs can arise is unclear. We exploited a hypermutagenic cancer cell line to select mutations conferring resistance to a well-studied Aurora inhibitor, ZM447439. All resistant clones contained dominant point mutations in Aurora B. Three mutations map to residues in the ATP-binding pocket that are distinct from the "gatekeeper" residue. The mutants retain wild-type catalytic activity and were resistant to all of the Aurora inhibitors tested. Our studies predict that drug-resistant Aurora B mutants are likely to arise during clinical treatment. Furthermore, because the plasticity of the ATP-binding pocket renders Aurora B insensitive to multiple inhibitors, our observations indicate that the drug-resistant Aurora B mutants should be exploited as novel drug targets.
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===STRUCTURE OF AURORA B KINASE IN COMPLEX WITH ZM447439===
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Molecular basis of drug resistance in aurora kinases.,Girdler F, Sessa F, Patercoli S, Villa F, Musacchio A, Taylor S Chem Biol. 2008 Jun;15(6):552-62. PMID:18559266<ref>PMID:18559266</ref>
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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 2vrx" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18559266}}, adds the Publication Abstract to the page
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*[[Centromere protein 3D structure|Centromere protein 3D structure]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18559266 is the PubMed ID number.
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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-->
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== References ==
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{{ABSTRACT_PUBMED_18559266}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2VRX 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=2VRX OCA].
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[[Category: Large Structures]]
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==Reference==
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Molecular basis of drug resistance in aurora kinases., Girdler F, Sessa F, Patercoli S, Villa F, Musacchio A, Taylor S, Chem Biol. 2008 Jun;15(6):552-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18559266 18559266]
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[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Protein complex]]
 
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Girdler, F.]]
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[[Category: Girdler, F]]
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[[Category: Musacchio, A.]]
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[[Category: Musacchio, A]]
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[[Category: Patercoli, S.]]
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[[Category: Patercoli, S]]
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[[Category: Ridgway, E.]]
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[[Category: Ridgway, E]]
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[[Category: Sessa, F.]]
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[[Category: Sessa, F]]
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[[Category: Taylor, S S.]]
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[[Category: Taylor, S S]]
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[[Category: Villa, F.]]
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[[Category: Villa, F]]
[[Category: Anti-cancer drug target]]
[[Category: Anti-cancer drug target]]
[[Category: Atp-binding]]
[[Category: Atp-binding]]
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[[Category: Cell cycle-transferase complex]]
[[Category: Cell cycle/transferase]]
[[Category: Cell cycle/transferase]]
[[Category: Cell division]]
[[Category: Cell division]]
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[[Category: Serine/threonine-protein kinase]]
[[Category: Serine/threonine-protein kinase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:12:11 2008''
 

Current revision

Structure of Aurora B kinase in complex with ZM447439

PDB ID 2vrx

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