EC Number   |
Inhibitors |
Structure  |
|---|
   5.6.1.3 | more |
synthetic peptides derived from the tail of kinesin inhibit the protein's ATPase and motor activities. A peptide that spans residues 904-933 exhibits the strongest inhibitory effect on steady-state motility and ATPase activity, reflecting diminished binding of the ADP-bound kinesin head to the microtubule. Tail-mediated inhibition of kinesin activity is mainly the product of allosteric inhibition induced by the intramolecular binding of kinesin tail domain to the motor domain |
 |
| 5.6.1.3 | more |
study of the discovery and optimization of hexahydro-2H-pyranol[3,2-c]quinolines, HHPQs, as inhibitors. Crystallographic data demonstrate that these potent and selectve inhibitors bind in an allosteric pocket of kinesin-5 distant from the nucleotide and microtubule binding sites; the activity assay for inhibition analysis are performed with a coupled ATP regeneration system with a total concentration of the kinesin-5 protein of approximately 50 nM in the reaction |
|
| 5.6.1.3 | more |
development of small molecule inhibitors of the enzyme Kif11 ATPase activity |
|
| 5.6.1.3 | more |
identification of optimized small molecule inhibitors of the mitotic kinesin Kif18A, usage of BTB-1 as a lead compound, structure-activity relationship studies and inhibition mechanism of BTB-1 and its analogues, overview |
|
| 5.6.1.3 | more |
kinesin performs autoinhibition, addition of a negative charge at Ser175 favors the autoinhibited conformation of kinesin |
|
| 5.6.1.3 | ADP |
- |
  |
| 5.6.1.3 | N-ethylmaleimide |
- |
|
| 5.6.1.3 | Calmodulin |
activated calmodulin inhibits KCBP interaction with microtubules thereby abolishing its motor- and microtubules-dependent ATPase activity |
|
| 5.6.1.3 | actin |
inhibition in the presence of microtubles |
|
| 5.6.1.3 | AMP-PNP |
binding structure |
|
