4ura
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of human JMJD2A in complex with compound 14a== |
| - | + | <StructureSection load='4ura' size='340' side='right' caption='[[4ura]], [[Resolution|resolution]] 2.23Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4ura]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4URA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=LEL:2-(2H-1,2,3-TRIAZOL-4-YL)PYRIDINE-4-CARBOXYLIC+ACID'>LEL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | + | <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=4ura FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ura OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ura RCSB], [http://www.ebi.ac.uk/pdbsum/4ura PDBsum]</span></td></tr> | |
| - | + | </table> | |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [[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> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arrowsmith, C H]] | ||
| + | [[Category: Bountra, C]] | ||
| + | [[Category: Brennan, P E]] | ||
[[Category: Burgess-Brown, N]] | [[Category: Burgess-Brown, N]] | ||
| + | [[Category: Crawley, L]] | ||
| + | [[Category: Edwards, A]] | ||
| + | [[Category: England, K S]] | ||
[[Category: Krojer, T]] | [[Category: Krojer, T]] | ||
| - | [[Category: Bountra, C]] | ||
| - | [[Category: Vollmar, M]] | ||
| - | [[Category: England, K.S]] | ||
| - | [[Category: Arrowsmith, C.H]] | ||
[[Category: Oppermann, U]] | [[Category: Oppermann, U]] | ||
| + | [[Category: Riesebos, E]] | ||
[[Category: Szykowska, A]] | [[Category: Szykowska, A]] | ||
| + | [[Category: Vollmar, M]] | ||
[[Category: Williams, E]] | [[Category: Williams, E]] | ||
| - | [[Category: | + | [[Category: VonDelft, F]] |
| - | [[Category: | + | [[Category: Histone demethylase]] |
| - | [[Category: | + | [[Category: Jumonjic]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
Revision as of 15:22, 17 June 2015
Crystal structure of human JMJD2A in complex with compound 14a
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