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purified recombinant isozyme 11beta-HSD1 in complex with substrate, cofactor and analogue, or inhibitor, 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 2mM Tris(carboxyethyl)phosphine, 5% glycerol, 0.5 M guanidinum hydrochloride, 0.05% Anapoe X-100, 0.02 mM cortisone, and 0.04 mM NADP+ analogue 3-aminopyridine adenine dinucleotide phosphate AADP, NADP+, BVT-4584, or cortisone, hanging drop vapour diffusion method, mixing with equal volume of precipitation solution containing 38-40% PEG 550 mono methyl ether, and 0.1 M Bis-Tris, pH 6.5, equlibration against 1 ml precipitation solution, 5-6 days, X-ray diffraction structure determination and analysis at 2.5 A resolution
analysis of substratebinding by threedimensional modeling. There are favorable interactions between the C7-hydroxyl group of substrate and the catalytic site when the A ring of substrate is oriented towards the interior of the enzyme
co-crystal structure of inhibitor 8-[[(2-cyanopyridin-3-yl)methyl]sulfanyl]-6-hydroxy-3,4-dihydro-1H-pyrano[3,4-c]pyridine-5-carbonitrile with enzyme and cofactor NADP+. Structure shows a critical H-bonding interaction between the OH pharmacophore of the inhibitor and the side chains of S170 and Y183 residues at the catalytic site of the enzyme
docking of cortisone into the catalytic site of wild type and mutant Y177A, PDB entry 2BEL. The catalytic site is stabilised in the enzyme dimer. Residues K44, N123, and T222 at the bottom of the cavity define a small functional back-door that allows water to enter or exit, making it easier for the substrate to leave or occupy the site. Residue Y177 is involved in stabilising interactions with the A ring of the substrate
in complex with inhibitor 2-[(3,3-dimethylpiperidin-1-yl)carbonyl]-6-(3-fluoro-4-methylphenyl)pyridine. The carbonyl oxygen of the inhibitor is within hydrogen bonding distance to active site residues S170 and Y183, the inhibitor also forms hydrophobic interactions with the protein
purified recombinant isozyme 11beta-HSD1 catalytic domain mutant C272S, the nanovolume crystallization method, the reservoir solution contains 20% PEG 3350, and 0.1 M MES, pH 6.2, soaking of crystals in 1 mM lutetium acetate reservoir solution, two crystal forms, X-ray diffraction structure determination and analysis at 1.55-2.45 A resolution
purified recombinant His6-tagged enzyme, hanging drop vapour diffusion method, 25 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 0.2 M NaCl, 0.1% Triton, 5% glycerol, and 2 mM EDTA, mixed with equal volume of well solution containing 1.8 M Li2O4, and 0.1 M HEOES, pH 7.5, at room temperature, derivatization with 1 mM ethylmercuric chloride, soaking of crystals with NADH and corticoserone containing solution, X-ray diffraction structure determination and analysis at 3.0 A resolution