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β-tubulin is a key subunit of tubulin heterodimers, which form microtubules essential for cell division, intracellular transport, and cell shape. The colchicine-binding site, located primarily on β-tubulin but at the α/β interface, is a target for various inhibitors. These inhibitors, including colchicine, bind to the site and prevent proper microtubule assembly, disrupting mitosis and cell function. Targeting this site is relevant in cancer chemotherapy and anti-inflammatory therapies, with the potential to overcome multidrug resistance.
Inhibitor binding prevents straight conformation needed for microtubule assembly, disrupting mitotic spindle formation and leading to cell cycle arrest.
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