ArticleBMC structural biology2010
A kinesin motor in a force-producing conformation.
Article in BMC structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.Biophysical journal · 2026Article
- Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.Scientific reports · 2026Article
- Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules.Scientific reports · 2022Article
- Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.Nature communications · 2018Article
- Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein.Scientific reports · 2017Article
- The structural switch of nucleotide-free kinesin.Scientific reports · 2017Article
- Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Remote control of myosin and kinesin motors using light-activated gearshifting.Nature nanotechnology · 2014Article
- ATP synthase: the right size base model for nanomotors in nanomedicine.TheScientificWorldJournal · 2014Review
- Kar3Vik1 mechanochemistry is inhibited by mutation or deletion of the C terminus of the Vik1 subunit.The Journal of biological chemistry · 2013Article
- Force generation by kinesin and myosin cytoskeletal motor proteins.Journal of cell science · 2013Review
- Article
- Neck rotation and neck mimic docking in the noncatalytic Kar3-associated protein Vik1.The Journal of biological chemistry · 2012Article
- Analyses of dynein heavy chain mutations reveal complex interactions between dynein motor domains and cellular dynein functions.Genetics · 2012Article
- Kar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern.The Journal of cell biology · 2012Article
- Altered nucleotide-microtubule coupling and increased mechanical output by a kinesin mutant.PloS one · 2012Article
- Article
- Neck-motor interactions trigger rotation of the kinesin stalk.Scientific reports · 2012Article
- Hysteresis-based mechanism for the directed motility of the Ncd motor.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundKinesin motors hydrolyze ATP to produce force and move along microtubules, converting chemical energy into work by a mechanism that is only poorly understood. Key transitions and intermediate states in the process are still structurally uncharacterized, and remain outstanding questions in the field. Perturbing the motor by introducing point mutations could stabilize transitional or unstable states, providing critical information about these rarer states.
resultsHere we show that mutation of a single residue in the kinesin-14 Ncd causes the motor to release ADP and hydrolyze ATP faster than wild type, but move more slowly along microtubules in gliding assays, uncoupling nucleotide hydrolysis from force generation. A crystal structure of the motor shows a large rotation of the stalk, a conformation representing a force-producing stroke of Ncd. Three C-terminal residues of Ncd, visible for the first time, interact with the central beta-sheet and dock onto the motor core, forming a structure resembling the kinesin-1 neck linker, which has been proposed to be the primary force-generating mechanical element of kinesin-1.
conclusionsForce generation by minus-end Ncd involves docking of the C-terminus, which forms a structure resembling the kinesin-1 neck linker. The mechanism by which the plus- and minus-end motors produce force to move to opposite ends of the microtubule appears to involve the same conformational changes, but distinct structural linkers. Unstable ADP binding may destabilize the motor-ADP state, triggering Ncd stalk rotation and C-terminus docking, producing a working stroke of the motor.
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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.