Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose).
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.
Eustermann
Sebastian
S
MRC Laboratory of Molecular Biology, Cambridge, UK.
Brockmann
Christoph
C
Mehrotra
Pawan Vinod
PV
Yang
Ji-Chun
JC
Loakes
David
D
West
Stephen C
SC
Ahel
Ivan
I
Neuhaus
David
D
D000595:Amino Acid Sequence; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism*; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism*; D000075223:Poly-ADP-Ribose Binding Proteins; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016335:Zinc Fingers
D010750:Phosphoproteins; D000075223:Poly-ADP-Ribose Binding Proteins; D011064:Poly Adenosine Diphosphate Ribose; C520557:APLF protein, human; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase