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 PubMedA series of benzofuran-based farnesyltransferase inhibitors have been designed and synthesized as antitumor agents. Among them, 11f showed the most potent enzyme inhibitory activity (IC(50)=1.1nM) and antitumor activity in human cancer xenografts in mice. Synthesis and structure-activity relationships of novel benzofuran farnesyltransferase inhibitors.,Asoh K, Kohchi M, Hyoudoh I, Ohtsuka T, Masubuchi M, Kawasaki K, Ebiike H, Shiratori Y, Fukami TA, Kondoh O, Tsukaguchi T, Ishii N, Aoki Y, Shimma N, Sakaitani M Bioorg Med Chem Lett. 2009 Mar 15;19(6):1753-7. Epub 2009 Feb 11. PMID:19217288[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 07:07, 18 October 2018.