Antimicrotubular drugs binding to vinca domain of tubulin

Mol Cell Biochem. 2003 Nov;253(1-2):41-7. doi: 10.1023/a:1026045100219.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antineoplastic Agents / chemistry*
  • Antineoplastic Agents / pharmacology
  • Binding Sites
  • Humans
  • Microtubules / drug effects
  • Microtubules / metabolism*
  • Protein Structure, Tertiary
  • Tubulin / metabolism*
  • Tubulin Modulators
  • Vinca Alkaloids / metabolism*
  • Vinca Alkaloids / pharmacology


  • Antineoplastic Agents
  • Tubulin
  • Tubulin Modulators
  • Vinca Alkaloids