ArticleBiophysical journal2005
Position and orientation of phalloidin in F-actin determined by X-ray fiber diffraction analysis.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 90 citations in OpenAlex.
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- Looking for Targets to Restore the Contractile Function in Congenital Myopathy Caused by GlnInternational journal of molecular sciences · 2020Article
- D-loop Dynamics and Near-Atomic-Resolution Cryo-EM Structure of Phalloidin-Bound F-Actin.Structure (London, England : 1993) · 2020Article
- Affimer proteins for F-actin: novel affinity reagents that label F-actin in live and fixed cells.Scientific reports · 2018Article
- β1-integrin-matrix interactions modulate cerebral microvessel endothelial cell tight junction expression and permeability.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2018Article
- High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Large-scale 3-dimensional quantitative imaging of tissues: state-of-the-art and translational implications.Translational research : the journal of laboratory and clinical medicine · 2017Review
- Dense small molecule labeling enables activator-dependent STORM by proximity mapping.Histochemistry and cell biology · 2016Article
- Quantitative nanoscale imaging of orientational order in biological filaments by polarized superresolution microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cofilin-induced cooperative conformational changes of actin subunits revealed using cofilin-actin fusion protein.Scientific reports · 2016Article
- Biochemical Activities of the Wiskott-Aldrich Syndrome Homology Region 2 Domains of Sarcomere Length Short (SALS) Protein.The Journal of biological chemistry · 2016Article
- A repeat unit of Vibrio diarrheal T3S effector subverts cytoskeletal actin homeostasis via binding to interstrand region of actin filaments.Scientific reports · 2015Article
- Synthetic chondramide A analogues stabilize filamentous actin and block invasion by Toxoplasma gondii.Journal of natural products · 2013Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Knowledge of the phalloidin binding position in F-actin and the relevant understanding of the mechanism of F-actin stabilization would help to define the structural characteristics of the F-actin filament. To determine the position of bound phalloidin experimentally, x-ray fiber diffraction data were obtained from well-oriented sols of F-actin and the phalloidin-F-actin complex. The differences in the layer-line intensity distributions, which were clearly observed even at low resolution (8 A), produced well-resolved peaks corresponding to interphalloidin vectors in the cylindrically averaged difference-Patterson map, from which the radial binding position was determined to be approximately 10 A from the filament axis. Then, the azimuthal and axial positions were determined by single isomorphous replacement phasing and a cross-Patterson map in radial projection to be approximately 84 degrees and 0.5 A relative to the actin mass center. The refined position was close to the position found by prior researchers. The position of rhodamine attached to phalloidin in the rhodamine-phalloidin-F-actin complex was also determined, in which the conjugated Leu(OH)(7) residue was found to face the outside of the filament. The position and orientation of the bound phalloidin so determined explain the increase in the interactions between long-pitch strands of F-actin and would also account for the inhibition of phosphate release, which might also contribute to the F-actin stabilization. The method of analysis developed in this study is applicable for the determination of binding positions of other drugs, such as jasplakinolide and dolastatin 11.
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