5var

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'''Unreleased structure'''
 
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The entry 5var is ON HOLD until Paper Publication
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==Crystal structure of KDM4A tandem TUDOR domain in complex with a tri-methyl lysine competitive inhibitor==
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<StructureSection load='5var' size='340' side='right' caption='[[5var]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5var]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VAR FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=92Y:(1R,2S,3R,4S)-3-[(dimethylamino)methyl]-1-phenylbicyclo[2.2.1]heptan-2-ol'>92Y</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5var FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5var OCA], [http://pdbe.org/5var PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5var RCSB], [http://www.ebi.ac.uk/pdbsum/5var PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5var ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref>
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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: Judge, R A]]
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[[Category: Upadhyay, A K]]
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[[Category: Kdm4a tandem tudor domain]]
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[[Category: Oxidoreductase]]

Revision as of 06:31, 28 March 2018

Crystal structure of KDM4A tandem TUDOR domain in complex with a tri-methyl lysine competitive inhibitor

5var, resolution 1.83Å

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