2N5N

Structure of an N-terminal domain of CHD4

Summary for 2N5N

• Entry DOI: 10.2210/pdb2n5n/pdb
• NMR Information: BMRB: 18906
• Descriptor: Chromodomain-helicase-DNA-binding protein 4 (1 entity in total)
• Functional Keywords: hmg-box-like domain, chd4, par-binding, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q14839
• Total number of polymer chains: 1
• Total formula weight: 9569.84

Authors

Silva, A.P.G.,Mackay, J.P. (deposition date: 2015-07-22, release date: 2015-11-18, Last modification date: 2024-05-15)

Primary citation

Silva, A.P.,Ryan, D.P.,Galanty, Y.,Low, J.K.,Vandevenne, M.,Jackson, S.P.,Mackay, J.P.
The N-terminal Region of Chromodomain Helicase DNA-binding Protein 4 (CHD4) Is Essential for Activity and Contains a High Mobility Group (HMG) Box-like-domain That Can Bind Poly(ADP-ribose).
J.Biol.Chem., 291:924-938, 2016

PubMed Abstract: 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 N-terminal region. The-fold consists of a four-α-helix bundle with structural similarity to the high mobility group 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.

PubMed: 26565020
DOI: 10.1074/jbc.M115.683227

Experimental method

SOLUTION NMR