Solution structure of a zinc-finger domain that binds to poly-ADP-ribose.

  title={Solution structure of a zinc-finger domain that binds to poly-ADP-ribose.},
  author={Shin Isogai and Shin-ichiro Kanno and Mariko Ariyoshi and Hidehito Tochio and Yutaka Ito and Akira Yasui and Masahiro Shirakawa},
  journal={Genes to cells : devoted to molecular & cellular mechanisms},
  volume={15 2},
Poly-ADP-ribosylation is a unique post-translational modification that controls various nuclear events such as repair of DNA single-strand breaks. Recently, the protein containing the poly-ADP-ribose (pADPr)-binding zinc-finger (PBZ) domain was shown to be a novel AP endonuclease and involved in a cell cycle checkpoint. Here, we determined the three-dimensional structure of the PBZ domain from Drosophila melanogaster CG1218-PA using NMR spectroscopy. The domain folds into a C2H2-type zinc… CONTINUE READING