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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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DNA-(Apurinic or Apyrimidinic Site) Lyase
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Humans
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Phosphoproteins / chemistry*
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Phosphoproteins / metabolism*
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Poly Adenosine Diphosphate Ribose / metabolism*
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Poly-ADP-Ribose Binding Proteins
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Protein Binding
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Protein Structure, Tertiary
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Zinc Fingers
Substances
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Phosphoproteins
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Poly-ADP-Ribose Binding Proteins
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Poly Adenosine Diphosphate Ribose
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APLF protein, human
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DNA-(Apurinic or Apyrimidinic Site) Lyase
Associated data
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PDB/2KQB
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PDB/2KQC
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PDB/2KQD
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PDB/2KQE