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J Biomol NMR. 2004 May;29(1):73-84
Authors: Mavoungou C, Israel L, Rehm T, Ksiazek D, Krajewski M, Popowicz G, Noegel AA, Schleicher M, Holak TA
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.
N-terminal Dbl domain of the RhoGEF, Kalirin
N-terminal Dbl domain of the RhoGEF, Kalirin
N-terminal Dbl domain of the RhoGEF, Kalirin
Content Type Journal Article
Category NMR structure note
Pages 1-8
DOI 10.1007/s10858-012-9605-x
Authors
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Abstract
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Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
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Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.
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NMR structural characterization of the N-terminal domain of the adenylyl cyclase-asso
Linear Mode
