Antimicrotubular drugs binding to vinca domain of tubulin.
Article Details
- CitationCopy to clipboard
Gupta S, Bhattacharyya B
Antimicrotubular drugs binding to vinca domain of tubulin.
Mol Cell Biochem. 2003 Nov;253(1-2):41-7.
- PubMed ID
- 14619954 [ View in PubMed]
- Abstract
Studies on vinca domain binding drugs were done in great details by a number of workers as it is recognized as a potential target for anticancer drug development. Their structures, properties, mode of action, success and failures as potential anticancer drug have been discussed in short details in this review. Among these drugs rhizoxin and maytansine are competitive inhibitors, and bind at the vinblastine binding site of tubulin where as others are non-competitive inhibitors. Besides binding, these drugs also differ in the extent of GTP hydrolysis, GTP exchange and in the stabilization of colchicine binding site. The toxicity level of these drugs towards the host cells and the extent of efflux of drugs by the P-glycoprotein mediated pump are also discussed.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Vinblastine Tubulin alpha-1A chain Protein Humans YesBinderDetails Vinblastine Tubulin beta chain Protein Humans YesBinderDetails Vinblastine Tubulin delta chain Protein Humans YesBinderDetails Vinblastine Tubulin epsilon chain Protein Humans YesBinderDetails Vinblastine Tubulin gamma-1 chain Protein Humans YesBinderDetails