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Kinesin motor proteins are a superfamily of ATP-dependent molecular motors that move unidirectionally along microtubules to transport cellular cargo, including organelles, vesicles, and proteins, and to participate in critical processes such as mitosis and meiosis[1][3][5][6][8]. Kinesins are typically composed of two heavy chains, forming dimeric or tetrameric complexes, and contain a conserved motor (head) domain that binds both microtubules and nucleotides, as well as variable coiled-coil stalks and cargo-binding tail regions[2][3][8]. Force for motility is generated by ATP hydrolysis in the head domain, enabling movement toward the microtubule plus end (anterograde transport), though some kinesins mediate retrograde movement or have non-motile functions[1][3][5][6][8]. Kinesin motor proteins are essential for cell viability; dysfunction or mutation is associated with neurodegenerative and mitotic diseases, and inhibition of mitotic kinesins is an active area of cancer therapeutics development[6][9].
Inhibition of ATPase activity (prevents energy transduction and movement along microtubules) Inhibition of microtubule binding or "walking" (arrests cargo transport and mitosis) Stabilization of inactive conformations (prevents the conformational changes required for motility)
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