Structural highlights
Function
[FNTA_RAT] Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity). [FNTB_RAT] Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A series of imidazole-containing biphenyls was prepared and evaluated in vitro for inhibition of FTase and cellular Ras processing. Several of these analogues, such as 21, are potent inhibitors of FTase (<1nM), FTase/GGTase selective (>300-fold) and cellularly active (<or=80nM). An X-ray crystal structure of inhibitor 21 bound to rat farnesyltransferase is also presented.
Novel and selective imidazole-containing biphenyl inhibitors of protein farnesyltransferase.,Curtin ML, Florjancic AS, Cohen J, Gu WZ, Frost DJ, Muchmore SW, Sham HL Bioorg Med Chem Lett. 2003 Apr 7;13(7):1367-71. PMID:12657284[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Curtin ML, Florjancic AS, Cohen J, Gu WZ, Frost DJ, Muchmore SW, Sham HL. Novel and selective imidazole-containing biphenyl inhibitors of protein farnesyltransferase. Bioorg Med Chem Lett. 2003 Apr 7;13(7):1367-71. PMID:12657284
