Binding of colchiceine to tubulin. Mechanisms of ligand association with tubulin.
Article Details
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Hastie SB, Macdonald TL
Binding of colchiceine to tubulin. Mechanisms of ligand association with tubulin.
Biochem Pharmacol. 1990 Apr 15;39(8):1271-6. doi: 10.1016/0006-2952(90)90002-3.
- PubMed ID
- 2322310 [ View in PubMed]
- Abstract
Colchiceine, a closely related structural analog of colchicine possessing a C-ring tropolone, has been shown to be a potent inhibitor of microtubule assembly in vitro (I50 = 20 microM). The mechanism of inhibition is mediated through binding to tubulin (KA = 1.2 +/- 0.7 x 10(4) M-1), although potentially not through the colchicine receptor site. Supporting the hypothesis of an alternate receptor are the observation of colchiceine binding to the isolated colchicine-tubulin complex (KA = 2.2 +/- 1.0 x 10(4) M-1), the poor correlation between the competitive inhibition of colchicine binding (KI = 125 microM) and the inhibition of microtubule assembly, and different structure-activity relationships for colchiceine analogs as compared to the colchicine series.
DrugBank Data that Cites this Article
- Drugs
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Colchiceine Tubulin alpha-1A chain Protein Humans UnknownBinderDetails Colchiceine Tubulin beta chain Protein Humans UnknownBinderDetails