化学
微管蛋白
秋水仙碱
结合位点
微管
微管聚合
生物化学
立体化学
小分子
血浆蛋白结合
蛋白质-蛋白质相互作用
生物物理学
计算生物学
结构-活动关系
组合化学
作用机理
细胞
生物活性
活动站点
酶
相似性(几何)
分子模型
聚合
真菌蛋白
作者
Luis Fernando Colorado-Pablo,Efrén Mar-Antonio,Guillermo Goode-Romero,Naomi S. Morrissette,Rodrigo Aguayo-Ortiz
标识
DOI:10.1021/acs.jmedchem.5c02701
摘要
Microtubules are key pharmacological targets in clinical and agricultural contexts. Their dynamic assembly is essential for cell function, making tubulin polymerization a prime target for treating cancer, inflammation, and parasitic diseases, as well as for use as herbicides and fungicides in agricultural applications. The colchicine binding site (COLbs) is among the most studied, known for binding structurally diverse compounds across three zones (Z1-Z3). All colchicine-site ligands bind the central region Z2, with some extending into Z1 or Z3, which differ in hydrophobicity and electronic properties. Here, we analyzed over 160 colchicine-site inhibitors from the Protein Data Bank, using the three-zone classification model to group them by molecular similarity and interaction profiles. This perspective highlights emerging mechanisms for COLbs ligands, including tubulin degradation, with the goal to inform the design of next-generation tubulin polymerization inhibitors.
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