ArticleThe Journal of biological chemistry2011
Loop L5 acts as a conformational latch in the mitotic kinesin Eg5.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Molecular docking and molecular dynamics investigation of novels thiazolopyrimidines binding to canonical and alternative allosteric sites of kinesin Eg5.Journal of molecular modeling · 2026Article
- Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5.Journal of chemical information and modeling · 2026Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- MD simulation-based screening approach identified tolvaptan as a potential inhibitor of Eg5.Molecular diversity · 2023Article
- Optical Control of Mitosis with a Photoswitchable Eg5 Inhibitor.Angewandte Chemie (International ed. in English) · 2022Article
- Using a comprehensive approach to investigate the interaction between Kinesin-5/Eg5 and the microtubule.Computational and structural biotechnology journal · 2022Article
- Cryo-EM structure of a microtubule-bound parasite kinesin motor and implications for its mechanism and inhibition.The Journal of biological chemistry · 2021Article
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Cryo-EM structure of the Ustilago maydis kinesin-5 motor domain bound to microtubules.Journal of structural biology · 2019Article
- Insights into the Molecular Mechanisms of Eg5 Inhibition by (+)-Morelloflavone.Pharmaceuticals (Basel, Switzerland) · 2019Article
- Cryo-EM Structure (4.5-Å) of Yeast Kinesin-5-Microtubule Complex Reveals a Distinct Binding Footprint and Mechanism of Drug Resistance.Journal of molecular biology · 2019Article
- Biallelic variants in KIF14 cause intellectual disability with microcephaly.European journal of human genetics : EJHG · 2018Article
- A posttranslational modification of the mitotic kinesin Eg5 that enhances its mechanochemical coupling and alters its mitotic function.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein.Scientific reports · 2017Article
- Article
- Src family kinase phosphorylation of the motor domain of the human kinesin-5, Eg5.Cytoskeleton (Hoboken, N.J.) · 2017Article
- The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.The Journal of biological chemistry · 2017Article
- Intraflagellar transport velocity is governed by the number of active KIF17 and KIF3AB motors and their motility properties under load.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Heterodimerization of Kinesin-2 KIF3AB Modulates Entry into the Processive Run.The Journal of biological chemistry · 2016Article
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Authors and funding
6 authors.
Funding
Abstract
All members of the kinesin superfamily of molecular motors contain an unusual structural motif consisting of an α-helix that is interrupted by a flexible loop, referred to as L5. We have examined the function of L5 in the mitotic kinesin Eg5 by combining site-directed mutagenesis of L5 with transient state kinetics, molecular dynamics simulations, and docking using cryo electron microscopy density. We find that mutation of a proline residue located at a turn within this loop profoundly slows nucleotide-induced structural changes both at the catalytic site as well as at the microtubule binding domain and the neck linker. Molecular dynamics simulations reveal that this mutation affects the dynamics not only of L5 itself but also of the switch I structural elements that sense ATP binding to the catalytic site. Our results lead us to propose that L5 regulates the rate of conformational change in key elements of the nucleotide binding site through its interactions with α3 and in so doing controls the speed of movement and force generation in kinesin motors.
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