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    Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose).

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    Authors
    Eustermann, Sebastian
    Brockmann, Christoph
    Mehrotra, Pawan Vinod
    Yang, Ji-Chun
    Loakes, David
    West, Stephen C
    Ahel, Ivan
    Neuhaus, David
    Affiliation
    MRC Laboratory of Molecular Biology, Cambridge, UK.
    Issue Date
    2010-02
    
    Metadata
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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.
    Citation
    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
    Journal
    Nature Structural & Molecular Biology
    URI
    http://hdl.handle.net/10541/109408
    DOI
    10.1038/nsmb.1747
    PubMed ID
    20098424
    Type
    Article
    Language
    en
    ISSN
    1545-9985
    ae974a485f413a2113503eed53cd6c53
    10.1038/nsmb.1747
    Scopus Count
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    All Paterson Institute for Cancer Research

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