Human MMP-12 catalytic domain in complex with*(R)-N*-Hydroxy-1-(phenethylsulfonyl)pyrrolidine-2-carboxamide

Contribution of ligand free energy of solvation to design new potent MMPs inhibitors.

Exploring the subtleties of drug-receptor interactions: the case of matrix metalloproteinases.

MME, Macrophage elastase, ME, hME, Matrix metalloproteinase-12, MMP-12

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAF
GPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG

0.1 M Tris-HCl, 30% PEG6000, 1 M LiCl, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor paramethoxy-sulfonyl-glycine hydroxamate

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-Hydroxy-2-(N-(2-hydroxyethyl)4-methoxyphenylsulfonamido)acetamide

Crystal structure of the catalytic domain of human mmp12 complexed with the inhibitor (S)-N-(2,3-dihydroxypropyl)-4-methoxy-N-(2-nitroso-2-oxoethyl)benzenesulfonamide

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor (R)-N-(3-hydroxy-1-nitroso-1-oxopropan-2-yl)-4-methoxybenzenesulfonamide

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-(2-nitroso-2-oxoethyl)biphenyl-4-sulfonamide

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-(2-nitroso-2-oxoethyl)benzenesulfonamide

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

MMP-12, Matrix, metalloproteinase, HYDROLASE-HYDROLASE INHIBITOR complex

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAF
GPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG