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Farnesyl protein transferase: a review of structural studies

C L Strickland1, P C Weber

  • 1Schering-Plough Research Institute, Kenilworth, NJ 07033-0539, USA.

Current Opinion in Drug Discovery & Development
|August 4, 2009
PubMed

Insights

Farnesyl protein transferase inhibitors offer a novel, non-cytotoxic approach to cancer treatment by blocking Ras protein modification. These mechanism-based inhibitors are crucial for developing more effective cancer therapies with fewer side effects.

Area of Science:

  • Oncology
  • Molecular Biology
  • Drug Discovery

Background:

  • Cancer therapies increasingly focus on targeting specific cell growth mechanisms.
  • Mechanism-based inhibitors aim for greater efficacy and reduced side effects compared to traditional treatments.
  • Ras proteins, crucial for cell function, are hyperactive in a significant portion of human cancers.

Purpose of the Study:

  • To review structural studies of farnesyl protein transferase (FPTase).
  • To discuss strategies for the discovery of FPTase inhibitors.
  • To highlight the role of FPTase inhibitors as emerging non-cytotoxic anticancer agents.

Main Methods:

  • Review of structural biology research on FPTase.
  • Analysis of drug discovery approaches for FPTase inhibitors.
  • Examination of clinical trial data for FPTase inhibitors.

Main Results:

  • Farnesyl protein transferase inhibitors prevent the farnesylation of Ras proteins.
  • This inhibition targets a key post-translational modification essential for Ras function.
  • FPTase inhibitors represent a promising class of non-cytotoxic anticancer agents.

Conclusions:

  • Targeting FPTase is a viable strategy for developing novel cancer treatments.
  • Structural insights into FPTase aid in the rational design of potent inhibitors.
  • Further development of FPTase inhibitors holds potential for improved cancer therapy outcomes.

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