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10 ns molecular dynamics simulations of inhibitor bound to isofrom AKR1C3. Binding could induce conformational changes to both inhibitor and enzyme. The compound presumably assumes a stable, energetically favored, planar conformation, with an estimated free energy of binding of -5 kcal/mol
docking of inhibitors (2E)-3-(4-methylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid, (2E)-3-(4-ethylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid, (2E)-3-(4-bromophenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid and (2E)-3-[4-(methylsulfanyl)phenyl]-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid to crystal structure. Compounds occupy a similar position of the active site as the co-crystallized indomethacin, with the Aryl1 overlapping with the p-chlorobenzoyl moiety of the indomethacin and the Aryl2 overlapping with an indole part of the indomethacin
in complex with inhibitor 3-[[4-(trifluoromethyl)phenyl]amino]benzoic acid. Compound adopts a similar binding orientation as flufenamic acid, however, its phenylamino ring projects deeper into a subpocket and confers selectivity over the other AKR1C isoforms
purified recombinant wild-type enzyme, hanging drop vapour diffusion method, 4°C, mixing of equal volumes of 14 mg/ml protein solution and mother liquor containing 0.1 M sodium citrate, pH 6.5, 0.1 M ammonium acetate, and 24-30% PEG 4000, cryoprotection of crystals in 20% ethylene glycol in mother liquor, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement study
purified enzyme with NADH, hanging drop vapour diffusion method, 4°C, in presence of 1.4 M ammonium sulfate, 0.14 M NaCl, and 0.1 M Tris, pH 9.0, rod cluster crystals appear within 1 week, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling