title: NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.
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.
authors.affiliation: Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
authors.forename: Chrystelle
authors.initials: C
authors.lastname: Mavoungou
authors.forename: Lars
authors.initials: L
authors.lastname: Israel
authors.forename: Till
authors.initials: T
authors.lastname: Rehm
authors.forename: Dorota
authors.initials: D
authors.lastname: Ksiazek
authors.forename: Marcin
authors.initials: M
authors.lastname: Krajewski
authors.forename: Grzegorz
authors.initials: G
authors.lastname: Popowicz
authors.forename: Angelika A
authors.initials: AA
authors.lastname: Noegel
authors.forename: Michael
authors.initials: M
authors.lastname: Schleicher
authors.forename: Tad A
authors.initials: TA
authors.lastname: Holak
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018797:Cell Cycle Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003598:Cytoskeletal Proteins / Q000737:chemistry*; D004023:Dictyostelium / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D013058:Mass Spectrometry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012694:Serine / Q000737:chemistry; D015398:Signal Transduction; D013696:Temperature; D014965:X-Rays
chemical_list: D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D012694:Serine