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

Nat Struct Mol Biol. 2010 Feb;17(2):241-3. doi: 10.1038/nsmb.1747. Epub 2010 Jan 24.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • Phosphoproteins
  • Poly-ADP-Ribose Binding Proteins
  • Poly Adenosine Diphosphate Ribose
  • APLF protein, human
  • DNA-(Apurinic or Apyrimidinic Site) Lyase

Associated data

  • PDB/2KQB
  • PDB/2KQC
  • PDB/2KQD
  • PDB/2KQE