Crystal structure of the complex between MMP-8 and a non-zinc chelating inhibitor

Extra Binding Region Induced by Non-Zinc Chelating Inhibitors into the S(1)' Subsite of Matrix Metalloproteinase 8 (MMP-8)

Structural basis for the highly selective inhibition of MMP-13

Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects

Crystal structures of novel non-peptidic, non-zinc chelating inhibitors bound to MMP-12

MMP-8 catalytic domain, UNP residues 100-262

Matrix metalloproteinase-8, MMP-8, PMNL collagenase, PMNL-CL

MLTPGNPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGI
LAHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQA
IYG

Hanging droplets were made by mixing 1.5-3.0ml of protein/inhibitor solution with 5ml of PEG solution (10% PEG6000, 0.2M Mes-NaOH, 0.02% NaN3, pH6.0). Droplets were concentrated against a reservoir buffer containing 1.0-2.0M sodium phosphate, 0.02% NaN3, pH6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal complexes of MMP-13 with non-zinc chelating inhibitors

Crystal complexes of MMP-12 with non-zinc chelating inhibitors

hydrolase, selective inhibition, non-zinc chelating inhibitors, Calcium, Collagen degradation, Extracellular matrix, Glycoprotein, Metal-binding, Metalloprotease, Polymorphism, Protease, Secreted, Zinc, Zymogen