ArticleStructure (London, England : 1993)2024
The mechanism and energetics of the dynein priming stroke.
Article in Structure (London, England : 1993), 2024. 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026Article
- What Determines the Directionality of Kinesins? Studying the Anomalous Directionality of Nonclaret Disjunctional Motor Mutants.Journal of the American Chemical Society · 2026Article
- Structural and ensemble-based mechanistic insights into cytoplasmic dynein-1.Frontiers in molecular biosciences · 2026Review
- A Practical Covariance-Based Method for Efficient Detection of Protein-Protein Attractive and Repulsive Interactions in Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025Article
- Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025Article
- On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Dyneins are an AAA+ motor responsible for motility and force generation toward the minus end of microtubules. Dynein motility is powered by nucleotide-dependent transitions of its linker domain, which transitions between straight (post-powerstroke) and bent (pre-powerstroke) conformations. To understand the dynamics and energetics of the linker, we performed all-atom molecular dynamics simulations of human dynein-2 primed for its power stroke. Simulations revealed that the linker can adopt either a bent conformation or a semi-bent conformation, separated by a 5.7 kT energy barrier. The linker cannot switch back to its straight conformation in the pre-powerstroke state due to a steric clash with the AAA+ ring. Simulations also showed that an isolated linker has a free energy minimum near the semi-bent conformation in the absence of the AAA+ ring, indicating that the linker stores energy as it bends and releases this energy during the powerstroke.
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Registered trials
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