ArticleInternational journal of molecular sciences2021
Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Neck region-microtubule interactions direct counterclockwise stepping of kinesin-1.Biophysical journal · 2026Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- Modeling Studies of the Mechanism of Context-Dependent Bidirectional Movements of Kinesin-14 Motors.Molecules (Basel, Switzerland) · 2024Article
- Causes, costs and consequences of kinesin motors communicating through the microtubule lattice.Journal of cell science · 2023Article
- Effect of varying load in moving period of a step on dynamics of molecular motors.The European physical journal. E, Soft matter · 2022Article
- Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The transition between strong and weak interactions of the kinesin head with the microtubule, which is regulated by the change of the nucleotide state of the head, is indispensable for the processive motion of the kinesin molecular motor on the microtubule. Here, using all-atom molecular dynamics simulations, the interactions between the kinesin head and tubulin are studied on the basis of the available high-resolution structural data. We found that the strong interaction can induce rapid large conformational changes of the tubulin, whereas the weak interaction cannot. Furthermore, we found that the large conformational changes of the tubulin have a significant effect on the interaction of the tubulin with the head in the weak-microtubule-binding ADP state. The calculated binding energy of the ADP-bound head to the tubulin with the large conformational changes is only about half that of the tubulin without the conformational changes.
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Registered trials
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