ArticleActa crystallographica. Section D, Biological crystallography2008
Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.
Article in Acta crystallographica. Section D, Biological crystallography, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Study of Cytotoxicity of 3-Azabicyclo[3.1.0]hexanes and Cyclopropa[International journal of molecular sciences · 2025Article
- Cardiac and skeletal actin substrates uniquely tune cardiac myosin strain-dependent mechanics.Open biology · 2018Article
- Coarse-graining provides insights on the essential nature of heterogeneity in actin filaments.Biophysical journal · 2012Article
- Actin structure and function.Annual review of biophysics · 2011Review
- Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation.Journal of molecular biology · 2010Article
- Crystal structures of monomeric actin bound to cytochalasin D.Journal of molecular biology · 2008Article
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Authors and funding
6 authors.
Funding
Abstract
The structure of actin in its monomeric form is known at high resolution, while the structure of filamentous F-actin is only understood at considerably lower resolution. Knowing precisely how the monomers of actin fit together would lead to a deeper understanding of the dynamic behavior of the actin filament. Here, a series of crystal structures of actin dimers are reported which were prepared by cross-linking in either the longitudinal or the lateral direction in the filament state. Laterally cross-linked dimers, comprised of monomers belonging to different protofilaments, are found to adopt configurations in crystals that are not related to the native structure of filamentous actin. In contrast, multiple structures of longitudinal dimers consistently reveal the same interface between monomers within a single protofilament. The reappearance of the same longitudinal interface in multiple crystal structures adds weight to arguments that the interface visualized is similar to that in actin filaments. Highly conserved atomic interactions involving residues 199-205 and 287-291 are highlighted.
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