Farnesyltransferase (FTase) is part of the prenyltransferase group. FTase modifies proteins by adding farnesyl diphosphate (FPP) – an isoprenoid lipid – to a cysteine in a CAAX motif near the C terminal. This addition forms a thioether linkage, makes the protein more hydrophobic and associates it with the membrane. Farnesylated proteins – like those of the Ras family - are involved in cellular signaling[1]
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Relevance
FTase inhibitors are being tested as anti-cancer agents.
Structural insights
FTase are composed of 2 subunits. The β subunit coordinates a Zn atom. The CAAX motif coordinates with the Zn+2 ion and the FPP coordinates with the β subunit[2].
