ArticleProtein engineering, design & selection : PEDS2016
Elastic properties of dynein motor domain obtained from all-atom molecular dynamics simulations.
Article in Protein engineering, design & selection : PEDS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Modelling nano-particle-PEG-NLS complexes for nucleus-targeted drug delivery: revisiting the multi-dynein nano-cargo transport on microtubules.Drug delivery · 2026Article
- The mechanism and energetics of the dynein priming stroke.Structure (London, England : 1993) · 2024Article
- Wave-like oscillations of clamped microtubules driven by collective dynein transport.Biophysical journal · 2024Article
- Regulatory mechanisms of the dynein-2 motility by post-translational modification revealed by MD simulation.Scientific reports · 2023Article
- Non-Ewald methods for evaluating the electrostatic interactions of charge systems: similarity and difference.Biophysical reviews · 2022Review
- Article
- Stochastic Model of T Cell Repolarization during Target Elimination I.Biophysical journal · 2020Article
- Thermal stability of single-domain antibodies estimated by molecular dynamics simulations.Protein science : a publication of the Protein Society · 2019Article
- Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations.PLoS computational biology · 2017Article
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6 authors at 4 institutions in 1 country.
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Abstract
Dyneins are large microtubule motor proteins that convert ATP energy to mechanical power. High-resolution crystal structures of ADP-bound cytoplasmic dynein have revealed the organization of the motor domain, comprising the AAA(+) ring, the linker, the stalk/strut and the C sequence. Recently, the ADP.vanadate-bound structure, which is similar to the ATP hydrolysis transition state, revealed how the structure of dynein changes upon ATP binding. Although both the ADP- and ATP-bound state structures have been resolved, the dynamic properties at the atomic level remain unclear. In this work, we built two models named 'the ADP model' and 'the ATP model', where ADP and ATP are bound to AAA1 in the AAA(+) ring, respectively, to observe the initial procedure of the structural change from the unprimed to the primed state. We performed 200-ns molecular dynamics simulations for both models and compared their structures and dynamics. The motions of the stalk, consisting of a long coiled coil with a microtubule-binding domain, significantly differed between the two models. The elastic properties of the stalk were analyzed and compared with the experimental results.
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