2n5n

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'''Unreleased structure'''
 
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The entry 2n5n is ON HOLD
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==Structure of an N-terminal domain of CHD4==
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<StructureSection load='2n5n' size='340' side='right'caption='[[2n5n]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n5n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N5N FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n5n OCA], [https://pdbe.org/2n5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n5n RCSB], [https://www.ebi.ac.uk/pdbsum/2n5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n5n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHD4_HUMAN CHD4_HUMAN] Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.<ref>PMID:9804427</ref> <ref>PMID:17626165</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Chromodomain Helicase DNA-binding protein 4 (CHD4) is a chromatin-remodeling enzyme that has been reported to regulate DNA damage responses through its N-terminal region in a poly(ADP-ribose) polymerase dependent manner. We have identified and determined the structure of a stable domain (CHD4-N) in this Nterminal region. The fold consists of a four alpha-helix bundle with structural similarity to the High Mobility Group (HMG) box, a domain that is well known as a DNA-binding module. We show that the CHD4-N domain binds with higher affinity to poly(ADP-ribose) than to DNA. We also show that the N-terminal region of CHD4, although not CHD4-N alone, is essential for full nucleosome remodeling activity and is important for localizing CHD4 to sites of DNA damage. Overall, these data build on our understanding of how CHD4/NuRD acts to regulate gene expression and participates in the DNA-damage response.
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Authors: Silva, A.P.G., Mackay, J.P.
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The N-terminal region of CHD4 is essential for activity and contains a HMG-box-like-domain that can bind poly(ADP-ribose).,Silva AP, Ryan DP, Galanty Y, Low JK, Vandevenne M, Jackson SP, Mackay JP J Biol Chem. 2015 Nov 12. pii: jbc.M115.683227. PMID:26565020<ref>PMID:26565020</ref>
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Description: Structure of an N-terminal domain of CHD4
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Silva, A.P.G]]
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<div class="pdbe-citations 2n5n" style="background-color:#fffaf0;"></div>
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[[Category: Mackay, J.P]]
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==See Also==
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*[[Chromodomain-helicase-DNA-binding protein 3D structures|Chromodomain-helicase-DNA-binding protein 3D structures]]
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*[[Helicase 3D structures|Helicase 3D structures]]
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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: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Mackay JP]]
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[[Category: Silva APG]]

Current revision

Structure of an N-terminal domain of CHD4

PDB ID 2n5n

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