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    Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains

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    Authors
    Lietzke, Susan E.
    Bose, Sahana
    Cronin, Thomas Charles
    Klarlund, Jes K.
    Chawla, Anil
    Czech, Michael P.
    Lambright, David G.
    UMass Chan Affiliations
    Program in Molecular Medicine
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2000-09-13
    Keywords
    1-Phosphatidylinositol 3-Kinase; Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Conserved Sequence; Crystallography, X-Ray; Inositol Phosphates; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphatidylinositols; Protein Conformation; Protein Structure, Secondary; Receptors, Cytoplasmic and Nuclear; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; src Homology Domains
    Life Sciences
    Medicine and Health Sciences
    
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    https://doi.org/10.1016/S1097-2765(00)00038-1
    Abstract
    Lipid second messengers generated by phosphoinositide (PI) 3-kinases regulate diverse cellular functions through interaction with pleckstrin homology (PH) domains in modular signaling proteins. The PH domain of Grp1, a PI 3-kinase-activated exchange factor for Arf GTPases, selectively binds phosphatidylinositol 3,4,5-trisphosphate with high affinity. We have determined the structure of the Grp1 PH domain in the unliganded form and bound to inositol 1,3,4,5-tetraphosphate. A novel mode of phosphoinositide recognition involving a 20-residue insertion within the beta6/beta7 loop explains the unusually high specificity of the Grp1 PH domain and the promiscuous 3-phosphoinositide binding typical of several PH domains including that of protein kinase B. When compared to other PH domains, general determinants of 3-phosphoinositide recognition and specificity can be deduced.
    Source

    Mol Cell. 2000 Aug;6(2):385-94.

    DOI
    10.1016/S1097-2765(00)00038-1
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/34048
    PubMed ID
    10983985
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    ae974a485f413a2113503eed53cd6c53
    10.1016/S1097-2765(00)00038-1
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