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5fwe
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==JMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H4(1-15)R3me2s PEPTIDE== | |
| - | + | <StructureSection load='5fwe' size='340' side='right' caption='[[5fwe]], [[Resolution|resolution]] 2.05Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5fwe]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWE FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[ | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=2MR:N3,+N4-DIMETHYLARGININE'>2MR</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=5fwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwe OCA], [http://pdbe.org/5fwe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwe RCSB], [http://www.ebi.ac.uk/pdbsum/5fwe PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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: Chowdhury, R]] | [[Category: Chowdhury, R]] | ||
| - | [[Category: Schofield, C | + | [[Category: Schofield, C J]] |
| - | [[Category: Walport, L | + | [[Category: Walport, L J]] |
| + | [[Category: 2-oxoglutarate]] | ||
| + | [[Category: Chromatin regulator]] | ||
| + | [[Category: Demethylase]] | ||
| + | [[Category: Dioxygenase]] | ||
| + | [[Category: Double-stranded beta helix]] | ||
| + | [[Category: Dsbh]] | ||
| + | [[Category: Epigenetic and transcription regulation]] | ||
| + | [[Category: Facial triad]] | ||
| + | [[Category: Histone]] | ||
| + | [[Category: Hydroxylation]] | ||
| + | [[Category: Iron]] | ||
| + | [[Category: Jmjc domain]] | ||
| + | [[Category: Jmjd2a]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Non-heme]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Oxygenase]] | ||
Revision as of 04:09, 12 May 2016
JMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H4(1-15)R3me2s PEPTIDE
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Categories: Chowdhury, R | Schofield, C J | Walport, L J | 2-oxoglutarate | Chromatin regulator | Demethylase | Dioxygenase | Double-stranded beta helix | Dsbh | Epigenetic and transcription regulation | Facial triad | Histone | Hydroxylation | Iron | Jmjc domain | Jmjd2a | Metal binding protein | Non-heme | Oxidoreductase | Oxygenase
