A structural change in the kinesin motor protein that drives motility

@article{Rice1999ASC,
  title={A structural change in the kinesin motor protein that drives motility},
  author={Sarah E. Rice and Abel W. Lin and Daniel Safer and Cynthia L. Hart and Nariman I. Naber and Bridget Carragher and Shane M. Cain and Elena Pechatnikova and Elizabeth M. Wilson-Kubalek and Michael Whittaker and Edward Pate and Roger M. Cooke and Edwin W. Taylor and Ronald A. Milligan and Ronald D. Vale},
  journal={Nature},
  year={1999},
  volume={402},
  pages={778-784}
}
Kinesin motors power many motile processes by converting ATP energy into unidirectional motion along microtubules. The force-generating and enzymatic properties of conventional kinesin have been extensively studied; however, the structural basis of movement is unknown. Here we have detected and visualized a large conformational change of a ∼15-amino-acid region (the neck linker) in kinesin using electron paramagnetic resonance, fluorescence resonance energy transfer, pre-steady state kinetics… 

ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy

An enhanced suite of single- and multiple-molecule fluorescence polarization microscopy assays are applied to report the orientation and mobility of kinesin molecules bound to microtubules as a function of nucleotide state.

Switch-based mechanism of kinesin motors

Docking of the ADP-bound and ATP-like crystallographic models of KIF1A into the corresponding cryo-electron microscopy maps suggests a rationale for the plus-end directional bias associated with the kinesin catalytic core.

Structure of a kinesin–tubulin complex and implications for kinesin motility

The X-ray structure of human kinesin-1 bound to αβ-tubulin is determined, which defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesIn motor domain from microtubules.

Structural links to kinesin directionality and movement

The kinesin motor proteins generate directional movement along microtubules and are involved in many vital processes, including cell division, in eukaryotes and recent work on chimeras and mutants is discussed in a structural context giving insights to possible molecular mechanisms of kinesIn directionality and motility.

Structural links to kinesin directionality and movement.

The kinesin motor proteins generate directional movement along microtubules and are involved in many vital processes, including cell division, in eukaryotes and recent work on chimeras and mutants is discussed in a structural context giving insights to possible molecular mechanisms of kinesIn directionality and motility.

How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1

The research on the mechanical pathway of energy transition and the regulating mechanism of the mechanochemical cycle of kinesin-1 is reviewed and the chemical and mechanical cycle are coupled to avoid futile nucleotide hydrolysis.

ESR reveals the mobility of the neck linker in dimeric kinesin.

Kinesin motility is driven by subdomain dynamics

The dynamic and wet kinesin-MT interface is tuned for rapid interactions while maintaining specificity, and provides the flexibility necessary for walking in the crowded cellular environment.
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