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TitleStructure of Microtubule-Trapped Human Kinesin-5 and Its Mechanism of Inhibition Revealed Using Cryoelectron Microscopy.
Journal, issue, pagesStructure, Vol. 28, Issue 4, Page 450-457.e5, Year 2020
Publish dateApr 7, 2020
AuthorsAlejandro Peña / Aaron Sweeney / Alexander D Cook / Julia Locke / Maya Topf / Carolyn A Moores /
PubMed AbstractKinesin-5 motors are vital mitotic spindle components, and disruption of their function perturbs cell division. We investigated the molecular mechanism of the human kinesin-5 inhibitor GSK-1, which ...Kinesin-5 motors are vital mitotic spindle components, and disruption of their function perturbs cell division. We investigated the molecular mechanism of the human kinesin-5 inhibitor GSK-1, which allosterically promotes tight microtubule binding. GSK-1 inhibits monomeric human kinesin-5 ATPase and microtubule gliding activities, and promotes the motor's microtubule stabilization activity. Using cryoelectron microscopy, we determined the 3D structure of the microtubule-bound motor-GSK-1 at 3.8 Å overall resolution. The structure reveals that GSK-1 stabilizes the microtubule binding surface of the motor in an ATP-like conformation, while destabilizing regions of the motor around the empty nucleotide binding pocket. Density corresponding to GSK-1 is located between helix-α4 and helix-α6 in the motor domain at its interface with the microtubule. Using a combination of difference mapping and protein-ligand docking, we characterized the kinesin-5-GSK-1 interaction and further validated this binding site using mutagenesis. This work opens up new avenues of investigation of kinesin inhibition and spindle perturbation.
External linksStructure / PubMed:32084356 / PubMed Central
MethodsEM (helical sym.)
Resolution3.8 - 6.1 Å
Structure data

10421

6ta3

6tiw

EMDB-10421: Human kinesin-5 motor domain in the GSK-1 state bound to microtubules
PDB-6ta3: Human kinesin-5 motor domain in the GSK-1 state bound to microtubules (Conformation 1)
PDB-6tiw: Human kinesin-5 motor domain in the GSK state bound to microtubules (Conformation 2)
Method: EM (helical sym.) / Resolution: 3.8 Å

10422

6ta4

EMDB-10422, PDB-6ta4:
Human kinesin-5 motor domain in the AMPPNP state bound to microtubules
Method: EM (helical sym.) / Resolution: 6.1 Å

Chemicals

ChemComp-G2P:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-CPP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-MZK:
6-[4-(trifluoromethyl)phenyl]-3,4-dihydro-1~{H}-quinolin-2-one

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • sus scrofa (pig)
  • homo sapiens (human)
  • Pig (pig)
KeywordsCELL CYCLE / kinesin / microtubule / mitosis / inhibition / motor

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