5c11

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'''Unreleased structure'''
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==Crystal Structure of Jarid1a PHD finger bound to histone H3C4me3 peptide==
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<StructureSection load='5c11' size='340' side='right' caption='[[5c11]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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The entry 5c11 is ON HOLD until Paper Publication
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5c11]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C11 FirstGlance]. <br>
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Authors: Huang, J., Li, H.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4WQ:(2S)-2-AMINO-7,7-DIMETHYLOCTANOIC+ACID'>4WQ</scene></td></tr>
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Description:
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c13|5c13]]</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=5c11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c11 OCA], [http://pdbe.org/5c11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c11 RCSB], [http://www.ebi.ac.uk/pdbsum/5c11 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/KDM5A_HUMAN KDM5A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May stimulate transcription mediated by nuclear receptors. May be involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity).[UniProtKB:Q3UXZ9]<ref>PMID:11358960</ref> <ref>PMID:15949438</ref> <ref>PMID:17320160</ref> <ref>PMID:17320161</ref> <ref>PMID:17320163</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Huang, J]]
[[Category: Huang, J]]
[[Category: Li, H]]
[[Category: Li, H]]
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[[Category: Demethylase]]
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[[Category: Hydrolase]]
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[[Category: Reader module]]
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[[Category: Zinc finger protein]]

Revision as of 04:43, 1 December 2015

Crystal Structure of Jarid1a PHD finger bound to histone H3C4me3 peptide

5c11, resolution 2.80Å

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