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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.

Original publication




Journal article


Nat Struct Mol Biol

Publication Date





241 - 243


Amino Acid Sequence, DNA-(Apurinic or Apyrimidinic Site) Lyase, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Phosphoproteins, Poly Adenosine Diphosphate Ribose, Poly-ADP-Ribose Binding Proteins, Protein Binding, Protein Structure, Tertiary, Zinc Fingers