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pubmed-article:20098424pubmed:abstractTextAddition 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.lld:pubmed
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pubmed-article:20098424pubmed:articleTitleSolution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose).lld:pubmed
pubmed-article:20098424pubmed:affiliationMRC Laboratory of Molecular Biology, Cambridge, UK.lld:pubmed
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