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Farnesyltransferase

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<StructureSection load='1tn7' size='350' side='right' scene='' caption='Rat farnesyltransferase α subunit (grey) and β subunit (green) complex with farnesyl diphosphate (FPP) analog, acetate and peptide (PDB code [[1tn7]]) '>
<StructureSection load='1tn7' size='350' side='right' scene='' caption='Rat farnesyltransferase α subunit (grey) and β subunit (green) complex with farnesyl diphosphate (FPP) analog, acetate and peptide (PDB code [[1tn7]]) '>
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to a Jmol applet. Check out the other buttons as well!
to a Jmol applet. Check out the other buttons as well!
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'''Farnesyltransferase''' (FTase) is part of the prenyltransferase group. FTase modifies proteins by adding farnesyl diphosphate (FPP) – an isoprenoid lipid – to a cysteine 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<ref>PMID:8747466</ref>
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'''Farnesyltransferase''' (FTase) is part of the prenyltransferase group. FTase modifies proteins by adding farnesyl diphosphate (FPP) – an isoprenoid lipid – to a cysteine in a CxxA 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<ref>PMID:15451670</ref>
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Revision as of 14:01, 21 January 2016

Rat farnesyltransferase α subunit (grey) and β subunit (green) complex with farnesyl diphosphate (FPP) analog, acetate and peptide (PDB code 1tn7)

Drag the structure with the mouse to rotate

3D structures of farnesyltransferase

Updated on 21-January-2016

References

  1. ↑ Reid TS, Terry KL, Casey PJ, Beese LS. Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J Mol Biol. 2004 Oct 15;343(2):417-33. PMID:15451670 doi:10.1016/j.jmb.2004.08.056

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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