EC Number   |
|---|
   3.4.24.B4 | a complex of human MMP-13 with bovine TIMP-2 is crystallized using the sitting-drop vapour diffusion method in 100 mM MES (pH 6.5), 200 mM magnesium acetate, 20% (w/v) PEG 8000 |
| 3.4.24.B4 | comparison of more than 40 X-ray co-crystal structures of the human MMP-13 with bound inhibitors to gain the structural insights such as conserved direct interactions with binding site residues, namely Ala-238, Thr-245 and Thr-247. Docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors |
| 3.4.24.B4 | crystal structures of catalytically inactive full-length MMP-13 mutant E223A in complex with peptides of 14-26 amino acids derived from the cleaved prodomain during activation. Peptides are bound to the active site of the enzyme by forming an extended beta-strand with Glu40 or Tyr46 inserted into the S1' specificity pocket |
| 3.4.24.B4 | enzyme catalytic domain in complex with inhibitor N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide, N,N'-bis(3-methylbenzyl)pyrimidine-4,6-dicarboxamide or N,N'-bis(4-fluoro-3-methylbenzyl)pyrimidine-4,6-dicarboxamide |
| 3.4.24.B4 | enzyme complexed with a hydroxamate inhibitor, hanging-drop vapour diffusion method, 17 mg/ml protein in 10 mM HEPES, pH 7.5, with ammonium sufate to saturation, 18°C, 60 days, X-ray diffraction structure determination at 2.0 A resolution, and analysis |
| 3.4.24.B4 | hanging drop vapor diffusion method, using 10% (w/v) PEG4000, 1 M ammonium formate, and 100 mM Tris, pH 8.0 |
| 3.4.24.B4 | in complex with inhibitor SM-25453, comparison with structure of EC 3.4.24.17 with inhibitor |
| 3.4.24.B4 | molecular dynamics simulations and multiway explorative data analysis on MMP13 complexed with Marimastat and two cis-1(S)2(R)-amino-2-indanol ligands, and comparison with proteases ADAMTS4, ADAMTS5. Determinant characteristics for ligand binding and selectivity among the three enzymes are to be found in the different protein conformation flexibility |
| 3.4.24.B4 | molecular modeling of binding of homochiral (3S,3S)-astaxanthin to enzyme |
| 3.4.24.B4 | recombinant enzyme, hanging-drop vapour diffusion method, 20 mM Tris-HCl, pH 7.3, 5 mM CaCl2, 300 mM NaCl, addition of 1 M ammonium sulfate solution, pH 9.0, equilibrated against ammonium sulfate at 1.2 M, 20°C, 1 week, X-ray structure determination at 2.7 A resolution and analyis of the C-terminal haemopexin-like domain |
