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  • Structural Evidence for Variable Oligomerization of the N-Terminal Domain of Cyclase-Associated Protein (CAP)

    Author(s)
    Yusof, AM
    Hu, NJ
    Wlodawer, A
    Hofmann, A
    Griffith University Author(s)
    Hofmann, Andreas
    Year published
    2005
    Metadata
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    Abstract
    Cyclase-associated protein (CAP) is a highly conserved and widely distributed protein that links the nutritional response signaling to cytoskeleton remodeling. In yeast, CAP is a component of the adenylyl cyclase complex and helps to activate the Ras-mediated catalytic cycle of the cyclase. While the N-terminal domain of CAP (NCAP) provides a binding site for adenylyl cyclase, the C-terminal domain (C-CAP) possesses actin binding activity. Our attempts to crystallize full-length recombinant CAP from Dictyostelium discoideum resulted in growth of orthorhombic crystals containing only the N-terminal domain (residues 42-227) ...
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    Cyclase-associated protein (CAP) is a highly conserved and widely distributed protein that links the nutritional response signaling to cytoskeleton remodeling. In yeast, CAP is a component of the adenylyl cyclase complex and helps to activate the Ras-mediated catalytic cycle of the cyclase. While the N-terminal domain of CAP (NCAP) provides a binding site for adenylyl cyclase, the C-terminal domain (C-CAP) possesses actin binding activity. Our attempts to crystallize full-length recombinant CAP from Dictyostelium discoideum resulted in growth of orthorhombic crystals containing only the N-terminal domain (residues 42-227) due to auto-proteolytic cleavage. The structure was solved by molecular replacement with data at 2.2A͊resolution. The present crystal structure allows the characterization of a head-to-tail N-CAP dimer in the asymmetric unit and a crystallographic side-toside dimer. Comparison with previously published structures of N-CAP reveals variable modes of dimerization of this domain, but the presence of a common interface for the side-to-side dimer.
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    Journal Title
    Proteins: Structure, Function, and Bioinformatics
    Volume
    58
    Subject
    Mathematical sciences
    Biological sciences
    Information and computing sciences
    Publication URI
    http://hdl.handle.net/10072/16740
    Collection
    • Journal articles

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