Kinesins are a family of microtubule-dependent motor proteins that carry cargoes such as vesicles, organelles, or protein complexes along microtubules. Here we summarize structural studies of the "conventional" motor protein kinesin-1 and its interactions with microtubules, as determined by X-ray crystallography and cryo-electron microscopy. In particular, we consider the docking between the kinesin motor domain and tubulin subunits and summarize the evidence that kinesin binds mainly to beta tubulin with the switch-2 helix close to the intradimer interface between alpha and beta tubulin
Microtubule-dependent motors of the kinesin family convert the energy from ATP hydrolysis into mecha...
Recently, the molecular structures of monomeric and dimeric kinesin constructs in complex with ADP h...
Microtubule-dependent motors of the kinesin family convert the energy from ATP hydrolysis into mecha...
Several X-ray crystal structures of kinesin motor domains have recently been solved at high resoluti...
The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtu...
International audienceThe typical function of kinesins is to transport cargo along microtubules. Bin...
AbstractKinesins are microtubule-dependent motors that serve a multitude of cellular purposes. The c...
International audienceMotile kinesins are motor proteins that move unidirectionally along microtubul...
Conventional kinesin (kinesin-1) transports membrane-bounded cargos such as mitochondria and vesicle...
Almost 25 years of kinesin research have led to the accumulation of a large bodyof knowledge about t...
An extensive computational analysis of available sequence and crystal structure data was used to ide...
Molecular motors often work collectively inside the cell. While the properties of individual motors ...
The binding stoichiometry of kinesin to microtubules was determined using several biochemical and bi...
We have used cryo-electron microscopy of kinesin-decorated microtubules to resolve the structure of ...
The microtubule motor kinesin-1 interacts via its cargo-binding domain with both microtubules and or...
Microtubule-dependent motors of the kinesin family convert the energy from ATP hydrolysis into mecha...
Recently, the molecular structures of monomeric and dimeric kinesin constructs in complex with ADP h...
Microtubule-dependent motors of the kinesin family convert the energy from ATP hydrolysis into mecha...
Several X-ray crystal structures of kinesin motor domains have recently been solved at high resoluti...
The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtu...
International audienceThe typical function of kinesins is to transport cargo along microtubules. Bin...
AbstractKinesins are microtubule-dependent motors that serve a multitude of cellular purposes. The c...
International audienceMotile kinesins are motor proteins that move unidirectionally along microtubul...
Conventional kinesin (kinesin-1) transports membrane-bounded cargos such as mitochondria and vesicle...
Almost 25 years of kinesin research have led to the accumulation of a large bodyof knowledge about t...
An extensive computational analysis of available sequence and crystal structure data was used to ide...
Molecular motors often work collectively inside the cell. While the properties of individual motors ...
The binding stoichiometry of kinesin to microtubules was determined using several biochemical and bi...
We have used cryo-electron microscopy of kinesin-decorated microtubules to resolve the structure of ...
The microtubule motor kinesin-1 interacts via its cargo-binding domain with both microtubules and or...
Microtubule-dependent motors of the kinesin family convert the energy from ATP hydrolysis into mecha...
Recently, the molecular structures of monomeric and dimeric kinesin constructs in complex with ADP h...
Microtubule-dependent motors of the kinesin family convert the energy from ATP hydrolysis into mecha...