The structural switch of nucleotide-free kinesin
L Cao, S Cantos-Fernandes, B Gigant - Scientific reports, 2017 - nature.com
Kinesin-1 is an ATP-dependent motor protein that moves towards microtubules (+)-ends.
Whereas structures of isolated ADP-kinesin and of complexes with tubulin of apo-kinesin
and of ATP-like-kinesin are available, structural data on apo-kinesin-1 in the absence of
tubulin are still missing, leaving the role of nucleotide release in the structural cycle
unsettled. Here, we identified mutations in the kinesin nucleotide-binding P-loop motif that
interfere with ADP binding. These mutations destabilize the P-loop (T87A mutant) or …
Whereas structures of isolated ADP-kinesin and of complexes with tubulin of apo-kinesin
and of ATP-like-kinesin are available, structural data on apo-kinesin-1 in the absence of
tubulin are still missing, leaving the role of nucleotide release in the structural cycle
unsettled. Here, we identified mutations in the kinesin nucleotide-binding P-loop motif that
interfere with ADP binding. These mutations destabilize the P-loop (T87A mutant) or …
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