ArticleBiophysical journal2003
EPR spectroscopy shows a microtubule-dependent conformational change in the kinesin switch 1 domain.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Remembering Roger Cooke (1940-2024): his life and science.Biophysical reviews · 2026Article
- Comparing the structural dynamics of the human KCNE3 in reconstituted micelle and lipid bilayered vesicle environments.Biochimica et biophysica acta. Biomembranes · 2022Article
- Plus and minus ends of microtubules respond asymmetrically to kinesin binding by a long-range directionally driven allosteric mechanism.Science advances · 2022Article
- Myosin and Other Energy-Transducing ATPases: Structural Dynamics Studied by Electron Paramagnetic Resonance.International journal of molecular sciences · 2020Review
- Shaft Function of Kinesin-1's α4 Helix in the Processive Movement.Cellular and molecular bioengineering · 2019Article
- Anchor Effect of Interactions Between Kinesin's Nucleotide-Binding Pocket and Microtubule.Cellular and molecular bioengineering · 2017Article
- Article
- Tau interconverts between diffusive and stable populations on the microtubule surface in an isoform and lattice specific manner.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Metal switch-controlled myosin II from Dictyostelium discoideum supports closure of nucleotide pocket during ATP binding coupled to detachment from actin filaments.The Journal of biological chemistry · 2013Article
- Conformational changes at the nucleotide site in the presence of bound ADP do not set the velocity of fast Drosophila myosins.Journal of muscle research and cell motility · 2013Article
- Reconstitution of KCNE1 into lipid bilayers: comparing the structural, dynamic, and activity differences in micelle and vesicle environments.Biochemistry · 2011Article
- Multiple conformations of the nucleotide site of Kinesin family motors in the triphosphate state.Journal of molecular biology · 2011Article
- An atomic-level mechanism for activation of the kinesin molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The Kinesin-1 tail conformationally restricts the nucleotide pocket.Biophysical journal · 2009Article
- The kinesin-1 motor protein is regulated by a direct interaction of its head and tail.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides.Biophysical journal · 2007Article
- ATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrol.Biochemistry · 2005Article
- Article
- A kinesin switch I arginine to lysine mutation rescues microtubule function.The Journal of biological chemistry · 2003Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
We have used site-directed spin-labeling and electron paramagnetic resonance spectroscopy to monitor a conformational change at the nucleotide site of kinesin. Cys-lite kinesin (K349 monomer) with the mutation S188C was spin labeled with MSL or MTSL. This residue is at the junction between the switch 1 region (which is a structure known to be sensitive to bound nucleotide in the G-proteins) and the alpha3-helix, adjacent to the nucleotide site. The spectra showed two or more components of mobility, which were independent of nucleotide in the absence of microtubules (MTs). The spectra of both labels showed a change of mobility upon binding to MTs. A more mobile spectral component became enhanced for all triphosphate analogs examined, AMPPNP, ADP.AlFx, or ADP.BeFx, in the presence of MTs, although the magnitude of the new component and the degree of mobility varied with nucleotide analog. The ADP state showed a much-reduced spectral change with a small shift to the more immobilized component in the presence of MTs. For kinesin.ADP.MT, a van't Hoff plot gave DeltaH degrees = -96 kJ/mol implying that the conformational change was extensive. We conclude there is a conformational change in the switch 1-alpha3-helix domain when kinesin binds to MTs.
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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.