ArticleProceedings of the National Academy of Sciences of the United States of America2010
The actin-myosin interface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 113 citations in OpenAlex.
- Thick filament molecular interfaces play a critical role in the pathogenesis of hypertrophic cardiomyopathy.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Exosomal miR-20a-5p derived from renal tubular epithelial cells regulates podocyte cytoskeletal remodeling via targeting myosin X in diabetic kidney disease.Diabetology & metabolic syndrome · 2026Article
- Exploring phosphoregulation of MYO3A using quantitative fluorescence image analysis in COS7 cells.microPublication biology · 2026Article
- Research reviews on myosin head interactions with F-actin.Applied microscopy · 2024Review
- Multiscale modeling shows how 2'-deoxy-ATP rescues ventricular function in heart failure.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Insights into Actin Isoform-Specific Interactions with Myosin via Computational Analysis.Molecules (Basel, Switzerland) · 2024Article
- Sequence Alignment-Based Prediction of Myosin 7A: Structural Implications and Protein Interactions.International journal of molecular sciences · 2024Article
- Similar proteome expression profiles of the aggregated lymphoid nodules area and Peyer's patches in Bactrian camel.BMC genomics · 2023Article
- Mechanisms of regulation of motility of the gastrointestinal tract and the hepatobiliary system under the chronic action of nanocolloids.Scientific reports · 2023Article
- Structural insights into actin isoforms.eLife · 2023Article
- Landscape-Based View on the Stepping Movement of Myosin VI.The journal of physical chemistry. B · 2022Article
- Divergent Plasmodium actin residues are essential for filament localization, mosquito salivary gland invasion and malaria transmission.PLoS pathogens · 2022Article
- The R369 Myosin Residue within Loop 4 Is Critical for Actin Binding and Muscle Function inInternational journal of molecular sciences · 2022Article
- Studies of functional properties of espin 1: Its interaction to actin filaments.Frontiers in cell and developmental biology · 2022Article
- Actomyosin Complex.Sub-cellular biochemistry · 2022Article
- Natural variant frequencies across domains from different sarcomere proteins cross-correlate to identify inter-protein contacts associated with cardiac muscle function and disease.Molecular biomedicine · 2021Article
- Myosin dilated cardiomyopathy mutation S532P disrupts actomyosin interactions, leading to altered muscle kinetics, reduced locomotion, and cardiac dilation inMolecular biology of the cell · 2021Article
- Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.Biophysical journal · 2019Article
- K336I mutant actin alters the structure of neighbouring protomers in filaments and reduces affinity for actin-binding proteins.Scientific reports · 2019Article
- Oxidative hotspots on actin promote skeletal muscle weakness in rheumatoid arthritis.JCI insight · 2019Article
8 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to understand the mechanism of muscle contraction at the atomic level, it is necessary to understand how myosin binds to actin in a reversible way. We have used a novel molecular dynamics technique constrained by an EM map of the actin-myosin complex at 13-A resolution to obtain an atomic model of the strong-binding (rigor) actin-myosin interface. The constraining force resulting from the EM map during the molecular dynamics simulation was sufficient to convert the myosin head from the initial weak-binding state to the strong-binding (rigor) state. Our actin-myosin model suggests extensive contacts between actin and the myosin head (S1). S1 binds to two actin monomers. The contact surface between actin and S1 has increased dramatically compared with previous models. A number of loops in S1 and actin are involved in establishing the interface. Our model also suggests how the loop carrying the critical Arg 405 Glu mutation in S1 found in a familial cardiomyopathy might be functionally involved.
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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.