4c2w: Difference between revisions

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New page: '''Unreleased structure''' The entry 4c2w is ON HOLD until Paper Publication Authors: Sessa, F., Villa, F. Description: Crystal structure of Aurora B in complex with AMP-PNP
 
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'''Unreleased structure'''


The entry 4c2w is ON HOLD  until Paper Publication
==Crystal structure of Aurora B in complex with AMP-PNP==
<StructureSection load='4c2w' size='340' side='right'caption='[[4c2w]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4c2w]] 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=4C2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C2W FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></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=4c2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c2w OCA], [https://pdbe.org/4c2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c2w RCSB], [https://www.ebi.ac.uk/pdbsum/4c2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c2w ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Aurora family is a well conserved and well characterized group of serine-threonine kinases involved in the normal progression of mitosis. The deregulation of Aurora kinases impairs spindle assembly, checkpoint function and cell division. To date, many small molecules that compete with ATP for binding to Aurora kinases have been developed and characterized. Here, the first structure of the Xenopus laevis Aurora B-INCENP complex bound to the clinically relevant small molecule barasertib was determined. The binding properties of this inhibitor to the Aurora B active site are analyzed and reported. An unexpected crystal-packing contact in the Aurora B-INCENP structure coordinated by an ATP analogue is also reported, in which the INCENP C-terminus occupies the substrate-binding region, resembling the protein kinase A inhibitory mechanism.


Authors: Sessa, F., Villa, F.
Structure of Aurora B-INCENP in complex with barasertib reveals a potential transinhibitory mechanism.,Sessa F, Villa F Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):294-8. doi:, 10.1107/S2053230X14002118. Epub 2014 Feb 19. PMID:24598913<ref>PMID:24598913</ref>


Description: Crystal structure of Aurora B in complex with AMP-PNP
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4c2w" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Centromere protein 3D structure|Centromere protein 3D structure]]
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Sessa F]]
[[Category: Villa F]]

Latest revision as of 02:44, 21 November 2024

Crystal structure of Aurora B in complex with AMP-PNP

4c2w, resolution 1.70Å

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