Farnesyltransferase
From Proteopedia
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| + | |||
| + | ===FTase=== | ||
[[1ft1]] – rFTase – rat<br /> | [[1ft1]] – rFTase – rat<br /> | ||
[[3q73]] – CnFTase – ''Cryptococcus neoformans'' | [[3q73]] – CnFTase – ''Cryptococcus neoformans'' | ||
| - | + | ===FTase binary complex with FPP=== | |
[[1ft2]], [[1fpp]] – rFTase + FPP<BR /> | [[1ft2]], [[1fpp]] – rFTase + FPP<BR /> | ||
[[1o1r]], [[1o1s]], [[3ksl]], [[3ksq]] - rFTase + FPP-analog<br /> | [[1o1r]], [[1o1s]], [[3ksl]], [[3ksq]] - rFTase + FPP-analog<br /> | ||
| - | + | ===FTase binary complex with peptide=== | |
[[1kzp]], [[1o1t]] - rFTase + farnesylated peptide<br /> | [[1kzp]], [[1o1t]] - rFTase + farnesylated peptide<br /> | ||
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[[3q79]] - CnFTase + farnesylated peptide | [[3q79]] - CnFTase + farnesylated peptide | ||
| - | + | ===FTase binary complex with inhibitor=== | |
[[3eu5]] – rFTase + biotin-GPP<br /> | [[3eu5]] – rFTase + biotin-GPP<br /> | ||
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[[1nl4]] - rFTase α subunit (mutant) + β subunit + inhibitor | [[1nl4]] - rFTase α subunit (mutant) + β subunit + inhibitor | ||
| - | + | ===FTase ternary complex with FPP and peptide=== | |
[[1d8d]], [[1tn8]] - rFTase + Ras peptide + FPP-analog<br /> | [[1d8d]], [[1tn8]] - rFTase + Ras peptide + FPP-analog<br /> | ||
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[[4l9p]] - AfFTase + peptide + FPP-analog – ''Apergillus fumigatus''<br /> | [[4l9p]] - AfFTase + peptide + FPP-analog – ''Apergillus fumigatus''<br /> | ||
| - | + | ===FTase ternary complex with FPP and inhibitor=== | |
[[1sa5]], [[3e30]], [[3e32]], [[3e33]], [[3e34]], [[3e37]] - rFTase + inhibitor + FPP<BR /> | [[1sa5]], [[3e30]], [[3e32]], [[3e33]], [[3e34]], [[3e37]] - rFTase + inhibitor + FPP<BR /> | ||
Revision as of 08:06, 18 August 2014
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. Thus, FTase inhibitors are being tested as anti-cancer agents. FTase are composed of 2 subunits. The β subunit coordinates a Zn atom.
Contents |
3D structures of farnesyltransferase
Updated on 18-August-2014
FTase
1ft1 – rFTase – rat
3q73 – CnFTase – Cryptococcus neoformans
FTase binary complex with FPP
1ft2, 1fpp – rFTase + FPP
1o1r, 1o1s, 3ksl, 3ksq - rFTase + FPP-analog
FTase binary complex with peptide
1kzp, 1o1t - rFTase + farnesylated peptide
2h6f - hFTase + farnesylated peptide
2h6g, 2h6h, 2h6i - hFTase α subunit + β subunit (mutant) + farnesylated peptide
3q79 - CnFTase + farnesylated peptide
FTase binary complex with inhibitor
3eu5 – rFTase + biotin-GPP
3euv - rFTase α subunit + β subunit (mutant)+ biotin-GPP
1n94, 1n95, 1n9a, 1o5m, 1ni1, 1x81, 2bed, 2r2l - rFTase + inhibitor
1nl4 - rFTase α subunit (mutant) + β subunit + inhibitor
FTase ternary complex with FPP and peptide
1d8d, 1tn8 - rFTase + Ras peptide + FPP-analog
1kzo - rFTase + farnesylated Ras peptide + FPP
1tn7, 3dpy - rFTase + peptide + FPP-analog
1jcr, 1jcs - rFTase + tetrapeptide inhibitor + FPP
1d8e - rFTase no Zn + Ras peptide + FPP-analog
1tn6 - hFTase + Rap2a peptide + FPP-analog
3q75, 3q78 - CnFTase + peptide + FPP-analog
4l9p - AfFTase + peptide + FPP-analog – Apergillus fumigatus
FTase ternary complex with FPP and inhibitor
1sa5, 3e30, 3e32, 3e33, 3e34, 3e37 - rFTase + inhibitor + FPP
2zir, 2zis - rFTase α subunit (mutant) + β subunit + inhibitor + FPP
1jcq – hFTase α subunit (mutant) + β subunit + inhibitor + FPP– human
1ld7, 1ld8, 1mzc, 1sa4, 1s63, 2f0y - hFTase + inhibitor + FPP
2iej - hFTase + inhibitor + FPP-analog
3pz4 - FTase + inhibitor + FPP – mouse
3q7a, 3q7f - CnFTase + inhibitor + FPP
3fsx, 3sfy - CnFTase + inhibitor + FPP-analog
4lnb, 4lng, 4mbg - AfFTase (mutant) + inhibitor + FPP
1n4p, 1n4r, 1n4s - rFTase α subunit + GTase β subunit + transforming protein + GPP
