Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs.

Abstract

Ras and Rho GTPases are prominent participants in malignant transformation. They possess an essential prenyl group (farnesyl or geranylgeranyl) that endows them with membrane-tethering ability and functional specificity. Accumulating evidence suggests that prenyl groups are involved primarily in lipid-protein interactions, and recent experiments point to prenyl-binding hydrophobic pockets in proteins regulating Ras and Rho in normal cells and cancer cells. This review presents the evidence for such prenyl-binding domains as significant players in the control of Ras-like GTPases, and the emerging concept of prenyl-binding domains as potential targets for Ras inhibitors and anti-cancer drugs.

• Authors: Yoel Kloog, Adrienne D Cox
• Journal: Seminars in cancer biology (Semin Cancer Biol) Vol. 14 Issue 4 Pg. 253-61 (Aug 2004) ISSN: 1044-579X [Print] England
• PMID: 15219618 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Review)

Chemical References

• ras Proteins

Topics

• Animals
• Binding Sites (drug effects)
• Gene Expression Regulation, Neoplastic (drug effects, physiology)
• Humans
• Neoplasms (therapy)
• Protein Prenylation
• ras Proteins (antagonists & inhibitors)