4.5 Article

Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)

Journal

NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 17, Issue 2, Pages 241-243

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1747

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Funding

  1. Boehringer Ingelheim Fonds
  2. Federation of European Biochemical Societies
  3. Cancer Research UK
  4. Louis-Jeantet Foundation
  5. Medical Research Council [MC_U105178934] Funding Source: researchfish
  6. MRC [MC_U105178934] Funding Source: UKRI

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Addition of poly(ADP-ribose) (PAR) is an important post-translational modification in higher eukaryotes. Several DNA repair and checkpoint proteins possess specific PAR-binding zinc-finger (PBZ) modules critical for function. Here, we present solution structures of the two PBZ modules of aprataxin and PNK-like factor (APLF), revealing a novel type of zinc finger. By combining in vivo PAR-binding data with NMR interaction data using PAR fragments, we propose a structural basis for PBZ-PAR recognition.

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