Farnesyltransferase
From Proteopedia
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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]]) '> | ||
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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. | + | '''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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| + | == Relevance == | ||
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| + | FTase inhibitors are being tested as anti-cancer agents. | ||
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| + | == Structural insights == | ||
| + | FTase are composed of 2 subunits. The β subunit coordinates a Zn atom. | ||
| + | </StructureSection> | ||
==3D structures of farnesyltransferase== | ==3D structures of farnesyltransferase== | ||
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**[[1n4p]], [[1n4r]], [[1n4s]] - rFTase α subunit + GTase β subunit + transforming protein + GPP<br /> | **[[1n4p]], [[1n4r]], [[1n4s]] - rFTase α subunit + GTase β subunit + transforming protein + GPP<br /> | ||
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| + | == References == | ||
| + | <references/> | ||
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 13:58, 21 January 2016
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3D structures of farnesyltransferase
Updated on 21-January-2016
References
- ↑ Athappilly FK, Hendrickson WA. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure. 1995 Dec 15;3(12):1407-19. PMID:8747466
