Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose).
Eustermann, Sebastian Brockmann, Christoph Mehrotra, Pawan Vinod Yang, Ji-Chun Loakes, David West, Stephen C Ahel, Ivan Neuhaus, David
Eustermann, Sebastian
Brockmann, Christoph
Mehrotra, Pawan Vinod
Yang, Ji-Chun
Loakes, David
West, Stephen C
Ahel, Ivan
Neuhaus, David
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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.
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Date
2010-02
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Article
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Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose). 2010, 17 (2):241-3 Nat Struct Mol Biol