NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum |
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Authors: | Chrystelle Mavoungou Lars Israel Till Rehm Dorota Ksiazek Marcin Krajewski Grzegorz Popowicz Angelika A Noegel Michael Schleicher Tad A Holak |
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Institution: | Max Planck Institute for Biochemistry, 82152 Martinsried, Germany. |
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Abstract: | Cyclase-associated proteins (CAPs) are highly conserved, ubiquitous actin binding proteins that are involved in microfilament reorganization. The N-termini of CAPs play a role in Ras signaling and bind adenylyl cyclase; the C-termini bind to G-actin. We report here the NMR characterization of the amino-terminal domain of CAP from Dictyostelium discoideum (CAP(1-226)). NMR data, including the steady state (1)H-(15)N heteronuclear NOE experiments, indicate that the first 50 N-terminal residues are unstructured and that this highly flexible serine-rich fragment is followed by a stable, folded core starting at Ser 51. The NMR structure of the folded core is an alpha-helix bundle composed of six antiparallel helices, in a stark contrast to the recently determined CAP C-terminal domain structure, which is solely built by beta-strands. |
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Keywords: | actin CAP cyclase-associated protein NMR structure |
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