NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.
Mavoungou, Chrystelle a; Israel, Lars b; Rehm, Till a; Ksiazek, Dorota a; Krajewski, Marcin a; Popowicz, Grzegorz a; Noegel, Angelika A. c; Schleicher, Michael b; Holak, Tad A. a
[Article] Journal of Biomolecular NMR. 29(1):73-84, May 2004.

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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 1H-15N 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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