|
|
| Line 1: |
Line 1: |
| | | | |
| | ==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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <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 [https://en.wikipedia.org/wiki/Human Human]. 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> | + | <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><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHD4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[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> | + | |
| | </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>
| + | [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 == |
| Line 25: |
Line 24: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mackay, J P]] | + | [[Category: Mackay JP]] |
| - | [[Category: Silva, A P.G]] | + | [[Category: Silva APG]] |
| - | [[Category: Chd4]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Hmg-box-like domain]]
| + | |
| - | [[Category: Par-binding]]
| + | |
| Structural highlights
Function
CHD4_HUMAN Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.[1] [2]
Publication Abstract from PubMed
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.
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 Also
References
- ↑ Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL. Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature. 1998 Oct 29;395(6705):917-21. PMID:9804427 doi:http://dx.doi.org/10.1038/27699
- ↑ Sillibourne JE, Delaval B, Redick S, Sinha M, Doxsey SJ. Chromatin remodeling proteins interact with pericentrin to regulate centrosome integrity. Mol Biol Cell. 2007 Sep;18(9):3667-80. Epub 2007 Jul 11. PMID:17626165 doi:http://dx.doi.org/10.1091/mbc.E06-07-0604
- ↑ Silva AP, Ryan DP, Galanty Y, Low JK, Vandevenne M, Jackson SP, Mackay JP. The N-terminal region of CHD4 is essential for activity and contains a HMG-box-like-domain that can bind poly(ADP-ribose). J Biol Chem. 2015 Nov 12. pii: jbc.M115.683227. PMID:26565020 doi:http://dx.doi.org/10.1074/jbc.M115.683227
|
