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| | ==Solution structure of CHD4-PHD2 in complex with H3K9me3== | | ==Solution structure of CHD4-PHD2 in complex with H3K9me3== |
| - | <StructureSection load='2l75' size='340' side='right' caption='[[2l75]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l75' size='340' side='right'caption='[[2l75]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l75]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L75 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l75]] is a 2 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=2L75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L75 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></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=2l75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l75 OCA], [https://pdbe.org/2l75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l75 RCSB], [https://www.ebi.ac.uk/pdbsum/2l75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l75 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHD4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2l75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l75 OCA], [http://pdbe.org/2l75 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l75 RCSB], [http://www.ebi.ac.uk/pdbsum/2l75 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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 == |
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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|Helicase]] | + | *[[Helicase 3D structures|Helicase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kwan, A H]] | + | [[Category: Large Structures]] |
| - | [[Category: Mackay, J P]] | + | [[Category: Kwan AH]] |
| - | [[Category: Mansfield, R E]] | + | [[Category: Mackay JP]] |
| - | [[Category: Chd4]] | + | [[Category: Mansfield RE]] |
| - | [[Category: H3k9me3]]
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| - | [[Category: Mi2b]]
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| - | [[Category: Phd2]]
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| - | [[Category: Transcription-nuclear protein complex]]
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| 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
A major challenge in chromatin biology is to understand the mechanisms by which chromatin is remodelled into active or inactive states as required during development and cell differentiation. One complex implicated in these processes is the Nucleosome Remodelling and histone Deacetylase (NuRD) complex, which contains both histone deacetylase and nucleosome remodelling activities and has been implicated in the silencing of subsets of genes involved in various stages of cellular development. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a core component of the NuRD complex, and contains a nucleosome remodelling ATPase domain along with two chromodomains and two plant homeodomain (PHD) fingers. We have previously demonstrated that the second PHD finger of CHD4 binds peptides corresponding to the N-terminus of histone H3 methylated at K9. Here, we determine the solution structure of PHD2 in complex with H3K9me3, revealing the molecular basis of histone recognition including a cation-pi recognition mechanism for methylated K9. Additionally we demonstrate that the first PHD finger also exhibits binding to the N-terminus of H3, and we establish the histone-binding surface of this domain. This is the first instance where a histone-binding ability has been demonstrated for two separate PHD modules within the one protein. These findings suggest that CHD4 could bind to two H3 N-terminal tails on the same nucleosome or on two separate nucleosomes simultaneously, presenting exciting implications for the mechanism by which CHD4 and the NuRD complex could direct chromatin remodelling.
The plant homeodomain (PHD) fingers of CHD4 are histone H3-binding modules with preference for unmodified H3K4 and methylated H3K9.,Mansfield RE, Musselman CA, Kwan AH, Garske AL, Davrazou F, Denu JM, Kutateladze TG, Mackay JP J Biol Chem. 2011 Jan 28. PMID:21278251[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
- ↑ Mansfield RE, Musselman CA, Kwan AH, Garske AL, Davrazou F, Denu JM, Kutateladze TG, Mackay JP. The plant homeodomain (PHD) fingers of CHD4 are histone H3-binding modules with preference for unmodified H3K4 and methylated H3K9. J Biol Chem. 2011 Jan 28. PMID:21278251 doi:10.1074/jbc.M110.208207
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