A structural change in the kinesin motor protein that drives motility
Article Abstract:
It has been possible to directly measure conformation of the kinesin neck linker in different nucleotide- and microtubule-binding states. This has formed the basis for a structural model of how kinesin moves along a microtubule. Fluorescence resonance energy transfer indicates that the neck linker experiences a large motion directed towards the tip of the catalytic core when microtubule-bound kinesin binds an ATP analogue. It was possible to devise a model for how ATP-induced neck linker docking can drive kinesin motility.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Direction determination in the minus-end-directed kinesin motor ncd
Article Abstract:
Kinesin superfamily motor proteins transport intracellular matter along microtubules. The ncd 'neck' comprising 13 class specific residues next to the superfamily-conserved catalytic core, is found to be necessary for minus-end-directed motility. The ncd neck is found to differ from corresponding regions in the kinesin neck, conferring different symmetries of the distinct neck architectures.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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How kinesin waits between steps
Article Abstract:
The development of two different single-molecule fluorescence resonance energy transfer (smFRET) sensor providing insight into hand-over-hand motion of kinesin-1 is reported. Kinesin is a dimeric motor protein that carrier cellular cargoes along microtubules mediated by transitions in the ATPase cycle.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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