2n5n: Difference between revisions
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==Structure of an N-terminal domain of CHD4== | ==Structure of an N-terminal domain of CHD4== | ||
<StructureSection load='2n5n' size='340' side='right' caption='[[2n5n | <StructureSection load='2n5n' size='340' side='right'caption='[[2n5n]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2n5n]] is a 1 chain structure with sequence from [ | <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> | ||
</td></tr> | </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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Chromodomain-helicase-DNA-binding protein|Chromodomain-helicase-DNA-binding protein]] | *[[Chromodomain-helicase-DNA-binding protein 3D structures|Chromodomain-helicase-DNA-binding protein 3D structures]] | ||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mackay JP]] | ||
[[Category: | [[Category: Silva APG]] | ||
Latest revision as of 12:56, 14 June 2023
Structure of an N-terminal domain of CHD4Structure of an N-terminal domain of CHD4
Structural highlights
FunctionCHD4_HUMAN Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.[1] [2] Publication Abstract from PubMedChromodomain 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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