ArticleThe Journal of biological chemistry2011
Loop 5-directed compounds inhibit chimeric kinesin-5 motors: implications for conserved allosteric mechanisms.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- 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
- 'Mitotic' kinesin-5 is a dynamic brake for axonal growth in Drosophila.Development (Cambridge, England) · 2025Article
- Cryo-EM structure of a microtubule-bound parasite kinesin motor and implications for its mechanism and inhibition.The Journal of biological chemistry · 2021Article
- Small molecule allosteric uncoupling of microtubule depolymerase activity from motility in human Kinesin-5 during mitotic spindle assembly.Scientific reports · 2019Article
- Cryo-EM structure of the Ustilago maydis kinesin-5 motor domain bound to microtubules.Journal of structural biology · 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
- Generating a "Humanized" Drosophila S2 Cell Line Sensitive to Pharmacological Inhibition of Kinesin-5.Journal of visualized experiments : JoVE · 2016Article
- Overexpression of Eg5 correlates with high grade astrocytic neoplasm.Journal of neuro-oncology · 2016Article
- Small molecule screen for candidate antimalarials targeting Plasmodium Kinesin-5.The Journal of biological chemistry · 2014Article
- Review
- Development of a Drosophila cell-based error correction assay.Frontiers in oncology · 2013Article
- The structural basis of force generation by the mitotic motor kinesin-5.The Journal of biological chemistry · 2012Article
- The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The human Eg5 (HsEg5) protein is unique in its sensitivity to allosteric agents even among phylogenetic kin. For example, S-trityl-l-cysteine (STC) and monastrol are HsEg5 inhibitors that bind to a surface pocket created by the L5 loop, but neither compound inhibits the Drosophila Kinesin-5 homologue (Klp61F). Herein we ask whether or not drug sensitivity can be designed into Klp61F. Two chimeric Klp61F motor domains were engineered, bacterially expressed, and purified to test this idea. We report that effector binding can elicit a robust allosteric response comparable with HsEg5 in both motor domain chimeras. Furthermore, isothermal titration calorimetry confirms that the Klp61F chimeras have de novo binding affinities for both STC and monastrol. These data show that the mechanism of intramolecular communication between the three ligand binding sites is conserved in the Kinesin-5 family, and reconstitution of a drug binding cassette within the L5 pocket is sufficient to restore allosteric inhibition. However, the two compounds were not equivalent in their allosteric inhibition. This surprising disparity in the response between the chimeras to monastrol and STC suggests that there is more than one allosteric communication network for these effectors.
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Registered trials
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.