Advances in the development of farnesyltransferase inhibitors: Substrate recognition by protein farnesyltransferase
A variety of compounds that show promise in cancer chemotherapy and chemoprevention have been identified as farnesyltransferase inhibitors. These can be classified into mainly two different types of inhibitors, farnesyl diphosphate competitors and CAAX peptidomimetics. The former type acts by compet...
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| Published in | Journal of cellular biochemistry Vol. 67; no. S27; pp. 12 - 19 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
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1997
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| Abstract | A variety of compounds that show promise in cancer chemotherapy and chemoprevention have been identified as farnesyltransferase inhibitors. These can be classified into mainly two different types of inhibitors, farnesyl diphosphate competitors and CAAX peptidomimetics. The former type acts by competitively inhibiting farnesyltransferase with respect to one of the substrates, farnesyl diphosphate, whereas the latter type acts by mimicking the other substrate, the C‐terminal CAAX motif of Ras protein. One example of a farnesyl diphosphate competitor is manumycin, an antibiotic detected in the culture media of a Streptomyces strain. The CAAX peptidomimetics were developed based on the unique property of farnesyltransferase to recognize the CAAX motif at the C‐terminus of the protein substrate. Our recent studies have focused on understanding the structural basis of this CAAX recognition. By using in vitro mutagenesis, residues of yeast farnesyltransferase important for the recognition of the CAAX motif have been identified. Two of these residues are closely located at the C‐terminal region of the β‐subunit of farnesyltransferase. These and other results on the structural basis of the CAAX recognition may provide information valuable for structure‐based design of farnesyltransferase inhibitors. J. Cell. Biochem. Suppl. 27:12–19. Published 1998 Wiley‐Liss, Inc. |
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| AbstractList | A variety of compounds that show promise in cancer chemotherapy and chemoprevention have been identified as farnesyltransferase inhibitors. These can be classified into mainly two different types of inhibitors, farnesyl diphosphate competitors and CAAX peptidomimetics. The former type acts by competitively inhibiting farnesyltransferase with respect to one of the substrates, farnesyl diphosphate, whereas the latter type acts by mimicking the other substrate, the C‐terminal CAAX motif of Ras protein. One example of a farnesyl diphosphate competitor is manumycin, an antibiotic detected in the culture media of a Streptomyces strain. The CAAX peptidomimetics were developed based on the unique property of farnesyltransferase to recognize the CAAX motif at the C‐terminus of the protein substrate. Our recent studies have focused on understanding the structural basis of this CAAX recognition. By using in vitro mutagenesis, residues of yeast farnesyltransferase important for the recognition of the CAAX motif have been identified. Two of these residues are closely located at the C‐terminal region of the β‐subunit of farnesyltransferase. These and other results on the structural basis of the CAAX recognition may provide information valuable for structure‐based design of farnesyltransferase inhibitors. J. Cell. Biochem. Suppl. 27:12–19. Published 1998 Wiley‐Liss, Inc. |
| Author | Del Villar, Keith Urano, Jun Yang, Wenli Tamanoi, Fuyuhiko Mitsuzawa, Hiroshi |
| Author_xml | – sequence: 1 givenname: Wenli surname: Yang fullname: Yang, Wenli organization: Department of Microbiology and Molecular Genetics, Jonsson Comprehensive Cancer Center, University of California, Los Angeles, California – sequence: 2 givenname: Keith surname: Del Villar fullname: Del Villar, Keith organization: Department of Microbiology and Molecular Genetics, Jonsson Comprehensive Cancer Center, University of California, Los Angeles, California – sequence: 3 givenname: Jun surname: Urano fullname: Urano, Jun organization: Department of Microbiology and Molecular Genetics, Jonsson Comprehensive Cancer Center, University of California, Los Angeles, California – sequence: 4 givenname: Hiroshi surname: Mitsuzawa fullname: Mitsuzawa, Hiroshi organization: Department of Molecular Genetics, National Institute of Genetics, Mishima, Japan – sequence: 5 givenname: Fuyuhiko surname: Tamanoi fullname: Tamanoi, Fuyuhiko organization: Department of Microbiology and Molecular Genetics, Jonsson Comprehensive Cancer Center, University of California, Los Angeles, California |
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contributor: fullname: Murphy |
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| Snippet | A variety of compounds that show promise in cancer chemotherapy and chemoprevention have been identified as farnesyltransferase inhibitors. These can be... |
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| Title | Advances in the development of farnesyltransferase inhibitors: Substrate recognition by protein farnesyltransferase |
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