Abstract
Farnesyltransferase (FTase) is a heterodimeric enzyme consisting of an α- and a β-subunit involved in a crucial C-terminal modification of various proteins, including Ras (1–3). This modification by a 15-carbon isoprenyl (farnesyl) group is essential for proper localization and function of these proteins (4–6). Because the membrane localization is necessary for Ras function, inhibiting FTase will prevent this localization, which in turn will block the ability of Ras to transform cells. Therefore, the structure and function of FTase has recently been intensively studied. Many studies have characterized substrate recognition by FTase in hope of being able to design small molecules that can act as anticancer drugs by specifically inhibiting this enzyme (1–7). Recently, the structure of the rat FTase has been solved (8).
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Urano, J., Tamanoi, F. (1998). Reconstitution of Yeast Farnesyltransferase from Individually Purified Subunits. In: Gelb, M.H. (eds) Protein Lipidation Protocols. Methods in Molecular Biology, vol 116. Humana Press. https://doi.org/10.1385/1-59259-264-3:145
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DOI: https://doi.org/10.1385/1-59259-264-3:145
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