5fwe

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'''Unreleased structure'''
 
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The entry 5fwe is ON HOLD
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==JMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H4(1-15)R3me2s PEPTIDE==
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<StructureSection load='5fwe' size='340' side='right' caption='[[5fwe]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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Authors: CHOWDHURY, R., Walport, L.J., SCHOFIELD, C.J.
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== Structural highlights ==
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<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>
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Description: JMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H4(1-15)R3me2s PEPTIDE
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</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>
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[[Category: Unreleased Structures]]
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<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>
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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=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>
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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>
[[Category: Chowdhury, R]]
[[Category: Chowdhury, R]]
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[[Category: Schofield, C.J]]
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[[Category: Schofield, C J]]
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[[Category: Walport, L.J]]
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[[Category: Walport, L J]]
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[[Category: 2-oxoglutarate]]
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[[Category: Chromatin regulator]]
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[[Category: Demethylase]]
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[[Category: Dioxygenase]]
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[[Category: Double-stranded beta helix]]
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[[Category: Dsbh]]
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[[Category: Epigenetic and transcription regulation]]
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[[Category: Facial triad]]
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[[Category: Histone]]
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[[Category: Hydroxylation]]
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[[Category: Iron]]
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[[Category: Jmjc domain]]
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[[Category: Jmjd2a]]
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[[Category: Metal binding protein]]
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[[Category: Non-heme]]
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[[Category: Oxidoreductase]]
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[[Category: Oxygenase]]

Revision as of 04:09, 12 May 2016

JMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H4(1-15)R3me2s PEPTIDE

5fwe, resolution 2.05Å

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