Farnesyltransferase
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FunctionFarnesyltransferase (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]. RelevanceFTase inhibitors are being tested as anti-cancer and anti-Progeria agents. Structural insightsFTase are composed of 2 subunits. α subunit is in cyan, β subunit is in green. CAAX peptide and ligands. The CAAX motif and β subunit coordinate with the Zn+2 ion and the FPP predominantly coordinates with the β subunit[2]. Water molecules are shown as red spheres. 3D structures of farnesyltransferaseFarnesyltransferase 3D structures
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This page was last modified 08:47, 26 June 2019.