Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 17, Issue 2, Pages 241-243Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1747
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Funding
- Boehringer Ingelheim Fonds
- Federation of European Biochemical Societies
- Cancer Research UK
- Louis-Jeantet Foundation
- Medical Research Council [MC_U105178934] Funding Source: researchfish
- MRC [MC_U105178934] Funding Source: UKRI
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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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