ArticleBiophysical journal1998
Nucleotide-dependent movements of the kinesin motor domain predicted by simulated annealing.
Article in Biophysical journal, 1998. 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, 36 citations in OpenAlex.
- Interaction of Tau with Kinesin-1: Effect of Kinesin-1 Heavy Chain Elimination on Autophagy-Mediated Mutant Tau Degradation.Biomedicines · 2023Article
- Flavin Binding to the Deca-heme Cytochrome MtrC: Insights from Computational Molecular Simulation.Biophysical journal · 2015Article
- Mapping the structural and dynamical features of kinesin motor domains.PLoS computational biology · 2013Article
- Analysis of the interaction of the Eg5 Loop5 with the nucleotide site.Journal of theoretical biology · 2011Article
- Myosin dynamics on the millisecond time scale.Biophysical chemistry · 2007Article
- Probing the local dynamics of nucleotide-binding pocket coupled to the global dynamics: myosin versus kinesin.Biophysical journal · 2005Article
- Article
- A comparative study of motor-protein motions by using a simple elastic-network model.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- A kinesin switch I arginine to lysine mutation rescues microtubule function.The Journal of biological chemistry · 2003Article
- Molecular dynamics simulations of the NGF-TrkA domain 5 complex and comparison with biological data.Biophysical journal · 2003Article
- Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules.The EMBO journal · 2001Article
- Molecular dynamics study of the energetic, mechanistic, and structural implications of a closed phosphate tube in ncd.Biophysical journal · 2001Article
- Domain motions of EF-G bound to the 70S ribosome: insights from a hand-shaking between multi-resolution structures.Biophysical journal · 2000Article
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2 authors at 1 institution in 1 country.
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Abstract
The structure of an ATP-bound kinesin motor domain is predicted and conformational differences relative to the known ADP-bound form of the protein are identified. The differences should be attributed to force-producing ATP hydrolysis. Candidate ATP-kinesin structures were obtained by simulated annealing, by placement of the ATP gamma-phosphate in the crystal structure of ADP-kinesin, and by interatomic distance constraints. The choice of such constraints was based on mutagenesis experiments, which identified Gly-234 as one of the gamma-phosphate sensing residues, as well as on structural comparison of kinesin with the homologous nonclaret disjunctional (ncd) motor and with G-proteins. The prediction of nucleotide-dependent conformational differences reveals an allosteric coupling between the nucleotide pocket and the microtubule binding site of kinesin. Interactions of ATP with Gly-234 and Ser-202 trigger structural changes in the motor domain, the nucleotide acting as an allosteric modifier of kinesin's microtubule-binding state. We suggest that in the presence of ATP kinesin's putative microtubule binding regions L8, L12, L11, alpha4, alpha5, and alpha6 form a face complementary in shape to the microtubule surface; in the presence of ADP, the microtubule binding face adopts a more convex shape relative to the ATP-bound form, reducing kinesin's affinity to the microtubule.
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