Article
The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.
Biophysical journal - 7 Dec 2011
Waitzman Joshua S, Larson Adam G, Cochran Jared C, Naber Nariman, Cooke Roger, Jon Kull F, Pate Edward, Rice Sarah E
Abstract excerpt
Eg5 is a homotetrameric kinesin-5 motor protein that generates outward force on the overlapping, antiparallel microtubules (MTs) of the mitotic spindle. Upon binding an MT, an Eg5 dimer releases one ADP molecule, undergoes a slow (∼0.5 s(-1)) isomerization, and finally releases a second ADP, adopting a tightly MT-bound, nucleotide-free (APO) conformation. This conformation precedes ATP binding and stepping. Here,...
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