Solution structure of the BRK domains from CHD7

J Mol Biol. 2007 Aug 31;371(5):1135-40. doi: 10.1016/j.jmb.2007.06.007. Epub 2007 Jun 9.


CHD7 is a member of the chromodomain helicase DNA binding domain (CHD) family of ATP-dependent chromatin remodelling enzymes. It is mutated in CHARGE syndrome, a multiple congenital anomaly condition. CHD7 is one of a subset of CHD proteins, unique to metazoans that contain the BRK domain, a protein module also found in the Brahma/BRG1 family of helicases. We describe here the NMR solution structure of the two BRK domains of CHD7. Each domain has a compact betabetaalphabeta fold. The second domain has a C-terminal extension consisting of two additional helices. The structure differs from those of other domains present in chromatin-associated proteins.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • DNA Helicases / chemistry*
  • DNA-Binding Proteins / chemistry*
  • Drosophila melanogaster
  • Glutathione Transferase / metabolism
  • Humans
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Molecular Conformation
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary


  • DNA-Binding Proteins
  • Ligands
  • Glutathione Transferase
  • DNA Helicases
  • CHD7 protein, human

Associated data

  • PDB/2V0E
  • PDB/2V0F