DNA repair: how Ku makes ends meet.
The recently determined crystal structure of the Ku heterodimer, in both DNA-bound and unbound forms, has shed new light on the mechanism by which this protein fulfills its key role in the repair of DNA double-strand breaks.
Doherty
A J
AJ
Cambridge Institute for Medical Research, Department of Haematology, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK. ajd42@cam.ac.uk
Jackson
S P
SP
D000818:Animals; D034961:Antigens, Nuclear; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004265:DNA Helicases; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D019281:Dimerization; D006801:Humans; D000072200:Ku Autoantigen; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D009690:Nucleic Acid Conformation; D017433:Protein Structure, Secondary
D034961:Antigens, Nuclear; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D004247:DNA; D004265:DNA Helicases; C106893:XRCC5 protein, human; C000606509:Xrcc6 protein, human; D000072200:Ku Autoantigen