ArticleJournal of biomolecular NMR2004
NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.
Article in Journal of biomolecular NMR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- CAPt'n of Actin Dynamics: Recent Advances in the Molecular, Developmental and Physiological Functions of Cyclase-Associated Protein (CAP).Frontiers in cell and developmental biology · 2020Review
- Autonomous and in trans functions for the two halves of Srv2/CAP in promoting actin turnover.Cytoskeleton (Hoboken, N.J.) · 2014Article
- The role of cyclase-associated protein in regulating actin filament dynamics - more than a monomer-sequestration factor.Journal of cell science · 2013Review
- Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin.Molecular biology of the cell · 2013Article
- CAS-1, a C. elegans cyclase-associated protein, is required for sarcomeric actin assembly in striated muscle.Journal of cell science · 2012Article
- Reconstitution and dissection of the 600-kDa Srv2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover.The Journal of biological chemistry · 2009Article
- The yeast actin cytoskeleton: from cellular function to biochemical mechanism.Microbiology and molecular biology reviews : MMBR · 2006Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
Indexed as
Identifiers
15017141What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.