Chromodomain-helicase-DNA-binding protein

Revision as of 10:42, 13 May 2019 by Michal Harel (talk | contribs)


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.[1]

  • CHD1 - ATP-dependent chromatin-modeling factor. Functions as substrate recognition component of the transcription regulatory acetylation complex SAGA.
  • CHD4 - Chromatin-modeling factor. Functions as component of the transcription regulatory deacetylation complex NuRD.
  • CHD6 - Probable transcription regulator.
  • CHD7 - ATP-dependent chromatin-modeling factor. May be involved in the 45S precursor ribosomal RNA production.
  • CHD8 - acts as transcription repressor by modeling chromatin structure and recruiting histone H1 to target genes.

Histone H3 tail peptide contains (PDB entry 2b2u).

3D structures of Chromodomain-helicase-DNA-binding protein

Chromodomain-helicase-DNA-binding protein 3D structures

Tandem chromodomains of human CHD1 (grey, green, pink) complex with histone H3 tail peptide (yellow) containing trimethyllysine and dimethylarginine (PDB entry 2b2u)

Drag the structure with the mouse to rotate

3D structures of CHD3D structures of CHD

Updated on 13-May-2019

ReferencesReferences

  1. Woodage T, Basrai MA, Baxevanis AD, Hieter P, Collins FS. Characterization of the CHD family of proteins. Proc Natl Acad Sci U S A. 1997 Oct 14;94(21):11472-7. PMID:9326634

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Michal Harel, Alexander Berchansky