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Chromodomain-helicase-DNA-binding protein: Difference between revisions

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<StructureSection load='2b2u' size='350' side='right' caption='Tandem chromodomains of human CHD1 (grey, green, pink) complex with histone H3 tail peptide (yellow) containing trimethyllysine and dimethylarginine (PDB entry [[2b2u]])' scene=''>
<StructureSection load='2b2u' size='350' side='right' caption='Tandem chromodomains of human CHD1 (grey, green, pink) complex with histone H3 tail peptide (yellow) containing trimethyllysine and dimethylarginine (PDB entry [[2b2u]])' scene='48/484850/Cv/1'>


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'''Chromodomain-helicase-DNA-binding proteins''' (CHD) remodel chromatin and histone deacylation thus affecting transcription.  Chromatin regulation involves the tightness of packing of DNA.  When DNA is tightly packed, gene expression is slower.  CHDs contain several domains such as chromodomain which is found in proteins involved in chromatin remodeling, PHD zinc finger which has Cys4-His-Cys3 motif and BRK domain which is associated with chromodomains.<ref>PMID:9326634</ref><br />
'''Chromodomain-helicase-DNA-binding proteins''' (CHD) remodel chromatin and histone deacylation thus affecting transcription.  Chromatin regulation involves the tightness of packing of DNA.  When DNA is tightly packed, gene expression is slower.  CHDs contain several domains such as chromodomain which is found in proteins involved in chromatin remodeling, PHD zinc finger which has Cys4-His-Cys3 motif and BRK domain which is associated with chromodomains.<ref>PMID:9326634</ref><br />
* '''CHD1''' - ATP-dependent chromatin-modeling factor. Functions as substrate recognition component of the transcription regulatory acetylation complex SAGA.<br />
* '''CHD1''' - ATP-dependent chromatin-modeling factor. Functions as substrate recognition component of the transcription regulatory acetylation complex SAGA.<br />
* '''CHD4''' - Chromatin-modeling factor.  Functions as component of the transcription regulatory deacetylation complex NuRD.<br />
* '''CHD4''' - Chromatin-modeling factor.  Functions as component of the transcription regulatory deacetylation complex NuRD. See [[Chromodomain helicase DNA-binding factor 4 (CHD4)]].<br />
* '''CHD5''' - belongs to ATP-dependent chromatin remodelling proteins.  It is a regulator of a tutor-suppressive network<ref>PMID:27096031</ref>.<br />
* '''CHD6''' - Probable transcription regulator.<br />
* '''CHD6''' - Probable transcription regulator.<br />
* '''CHD7''' - ATP-dependent chromatin-modeling factor.  May be involved in the 45S precursor ribosomal RNA production.<br />
* '''CHD7''' - ATP-dependent chromatin-modeling factor.  May be involved in the 45S precursor ribosomal RNA production.<br />
* '''CHD8''' - acts as transcription repressor by modeling chromatin structure and recruiting histone H1 to target genes.
* '''CHD8''' - acts as transcription repressor by modeling chromatin structure and recruiting histone H1 to target genes.
</StructureSection>


==3D structures of CHD==
Histone H3 tail peptide contains <scene name='48/484850/Cv/4'>trimethyllysine and dimethylarginine</scene> (PDB entry [[2b2u]]).


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
==3D structures of Chromodomain-helicase-DNA-binding protein==
[[Chromodomain-helicase-DNA-binding protein 3D structures]]
</StructureSection>


[[2b2t]] – hCHD1 (mutant) + histone H3 tail – human<br />
[[2b2u]], [[2b2v]], [[2b2w]] - hCHD1 + histone H3 tail<br />
[[2b2y]] - hCHD1 chromodomains<br />
[[4b4c]] – hCHD1 DNA-binding domain<br />
[[4nw2]] - hCHD1 chromodomains + nonstructural protein<br />
[[2l5u]] – hCHD4 PHD finger 1 – NMR<br />
[[2l75]] - hCHD4 PHD finger 2 + histone H3 peptide – NMR<br />
[[2ee1]] – hCHD4 chromodomain  – NMR<br />
[[1mm2]], [[1mm3]] - hCHD4 PHD finger 2 – NMR<br />
[[2epb]] – hCHD6 chromodomain 2 – NMR<br />
[[2ckc]], [[2v0e]], [[2v0f]] – hCHD7 BRK domain - NMR<br />
[[2dl6]], [[2cka]] – hCHD8 BRK domain - NMR
== References ==
== References ==
<references/>
<references/>


[[Category:Topic Page]]
[[Category:Topic Page]]

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Michal Harel, Alexander Berchansky
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