ArticleProceedings of the National Academy of Sciences of the United States of America2005
The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 56 citations in OpenAlex.
- New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles ofInternational journal of molecular sciences · 2020Article
- Single-molecule nanopore sensing of actin dynamics and drug binding.Chemical science · 2019Article
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- G-actin guides p53 nuclear transport: potential contribution of monomeric actin in altered localization of mutant p53.Scientific reports · 2016Article
- Archaeal actin from a hyperthermophile forms a single-stranded filament.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Computational prediction of actin-actin interaction.Molecular biology reports · 2014Article
- Cofilin-induced changes in F-actin detected via cross-linking with benzophenone-4-maleimide.Biochemistry · 2013Article
- Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural polymorphism in F-actin.Nature structural & molecular biology · 2010Article
- Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation.Journal of molecular biology · 2010Article
- WDR11, a WD protein that interacts with transcription factor EMX1, is mutated in idiopathic hypogonadotropic hypogonadism and Kallmann syndrome.American journal of human genetics · 2010Article
- Mechanical distortion of single actin filaments induced by external force: detection by fluorescence imaging.Biophysical journal · 2009Article
- Article
- X-ray scattering study of actin polymerization nuclei assembled by tandem W domains.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Interactions between the yeast SM22 homologue Scp1 and actin demonstrate the importance of actin bundling in endocytosis.The Journal of biological chemistry · 2008Article
- Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.Acta crystallographica. Section D, Biological crystallography · 2008Article
- Flavonoids affect actin functions in cytoplasm and nucleus.Biophysical journal · 2007Article
- Nucleotide effects on the structure and dynamics of actin.Biophysical journal · 2007Article
- Three-dimensional structure of cofilin bound to monomeric actin derived by structural mass spectrometry data.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Actin filament severing by cofilin.Journal of molecular biology · 2007Article
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7 authors at 2 institutions in 2 countries.
Funding
Abstract
The 2.5-A resolution crystal structure is reported for an actin dimer, composed of two protomers cross-linked along the longitudinal (or vertical) direction of the F-actin filament. The crystal structure provides an atomic resolution view of a molecular interface between actin protomers, which we argue represents a near-native interaction in the F-actin filament. The interaction involves subdomains 3 and 4 from distinct protomers. The atomic positions in the interface visualized differ by 5-10 A from those suggested by previous models of F-actin. Such differences fall within the range of uncertainties allowed by the fiber diffraction and electron microscopy methods on which previous models have been based. In the crystal, the translational arrangement of protomers lacks the slow twist found in native filaments. A plausible model of F-actin can be constructed by reintroducing the known filament twist, without disturbing significantly the interface observed in the actin dimer crystal.
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