Solution structure of the BRK domains from CHD7.
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.
Allen
Mark D
MD
MRC Centre for Protein Engineering, Hills Road, Cambridge, CB2 2QH, UK.
Religa
Tomasz L
TL
Freund
Stefan M V
SM
Bycroft
Mark
M
D000595:Amino Acid Sequence; D000818:Animals; D004265:DNA Helicases / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004331:Drosophila melanogaster; D005982:Glutathione Transferase / Q000378:metabolism; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D004268:DNA-Binding Proteins; D008024:Ligands; D005982:Glutathione Transferase; D004265:DNA Helicases; C491434:CHD7 protein, human