1n94 | pdb_00001n94

Aryl Tetrahydropyridine Inhbitors of Farnesyltransferase: Glycine, Phenylalanine and Histidine Derivates

spinqualitylabelsall models 1n94, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1n94 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Ligands: HFP, TIN, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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 Inhibitors of farnesyltransferase are effective against a variety of tumors in mouse models of cancer. Clinical trials to evaluate these agents in humans are ongoing. In our effort to develop new farnesyltransferase inhibitors, we have discovered a series of aryl tetrahydropyridines that incorporate substituted glycine, phenylalanine and histidine residues. The design, synthesis, SAR and biological properties of these compounds will be discussed. Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine, phenylalanine and histidine derivatives.,Gwaltney SL 2nd, O'Connor SJ, Nelson LT, Sullivan GM, Imade H, Wang W, Hasvold L, Li Q, Cohen J, Gu WZ, Tahir SK, Bauch J, Marsh K, Ng SC, Frost DJ, Zhang H, Muchmore S, Jakob CG, Stoll V, Hutchins C, Rosenberg SH, Sham HL Bioorg Med Chem Lett. 2003 Apr 7;13(7):1359-62. PMID:12657282 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Farnesyltransferase 3D structures

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