ArticleJournal of chemical information and modeling2026
Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5.
Article in Journal of chemical information and modeling, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Human kinesin-5 is a protein that oversees the proper formation of the bipolar mitotic spindle and is thus an appealing target for cancer treatment. The main group of kinesin-5 inhibitors reported to date binds to an allosteric pocket formed by loop 5 (L5), which is a key structural element believed to allosterically modulate kinesin-5 functionality. In this study, we carried out extensive molecular dynamics (MD) simulations on the motor domain of kinesin-5 in four representative catalytic states: ATP-bound, ADP-bound, without nucleotide (apo), and dually bound by ADP and the known main group inhibitor filanesib. MD trajectories were analyzed using the
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