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    A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1

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    Authors
    Kahn, Richard A.
    Lambright, David G.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    2015-11-03
    Keywords
    Biochemistry
    Molecular Biology
    Structural Biology
    
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    Link to Full Text
    http://dx.doi.org/10.1016/j.str.2015.10.002
    Abstract
    In this issue of Structure, Jian et al. (2015) report the crystal structures of the apo- and dibutyryl-PI(4,5)P2 bound forms of the PH domain from the ARF GAP, ASAP1. This PH domain has two anionic phospholipid binding sites proposed to work in concert to regulate ASAP1 GAP activity.
    Source
    Structure. 2015 Nov 3;23(11):1971-3. doi: 10.1016/j.str.2015.10.002. Link to article on publisher's site
    DOI
    10.1016/j.str.2015.10.002
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/44461
    PubMed ID
    26536378
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.str.2015.10.002
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