EC Number   |
|---|
   2.7.11.24 | bilobal structure analysis |
| 2.7.11.24 | crystal structure analysis of ERK2, PDB ID 1ERK |
| 2.7.11.24 | crystal structure of p38alpha, show docking grooves for binding of substrate D-domains, i.e. of MEF2A, and of activating kinases, e.g. of MKK3b, Ile116 and Gln120 play important roles |
| 2.7.11.24 | crystal structure of the unphosphorylated p38alpha-MK2, by hanging drop method, full-length p38alpha-MK2 complex to 4 A resolution, belongs to spacegroup P41 with unit cell dimensions of 103.09 A, 103.09 A, 231.42 A, 90.0°, 90.0°, 90.0°, p38alpha-MK2 peptide complex, belongs to spacegroup P31 with unit cell dimensions of 81.55 A, 81.55 A, 121.36 A, 90.0°, 90.0°, 120.0°. C-terminal regulatory domain of MK2 binds in the docking groove of p38alpha, and the ATP-binding sites of both kinases are at the heterodimer interface |
| 2.7.11.24 | ERK2, X-ray diffraction structure analysis |
| 2.7.11.24 | isolated PDZ domain of protein tyrosine phosphatase non-receptor type bound to the p38gamma C-terminus, i.e. Cyto8-RETEV and p38gamma-KETPL peptides, mixing of the protein ligand solution from 5 mg/ml PTPN4-PDZ domain and the appropriate peptide at a ratio of 1:2 and 1:4 for PTPN4-PDZCyto8-RETEV and PTPN4-PDZp38gamma-KETPL, respectively, in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.5 mM TCEP, sitting drop vapor diffusion method, mixing of 400 nl protein-ligand solution with 200 nl of precipitant solution containing 23% PEG 8000, 100 mM MES, pH 6.0, 200 mM calcium acetate, 0.143 mM ammonium sulfate or 1.2 M sodium dihydrogen phosphate, 0.8 M dipotassium hydrogen phosphate, 0.1 M CAPS, pH 10.5, 0.2 M lithium sulfate, 0.67 M non-detergent sulfobetaine (NDSB) 201, 18°C, X-ray diffraction structure determination and analysis at 2.09-2.35 A resolution, modeling |
| 2.7.11.24 | p38alpha active mutants crystallized by sitting-drop vapour-diffusion method, mutant D176A/F327L to 1.45 A resolution, crystals of the three p38alpha mutants belong to the orthorhombic space group P212121, with one molecule in the asymmetric unit |
| 2.7.11.24 | purified p38 isozyme alpha bound to several inhibitors pyridinyl imidazole-type inhibitors, X-ray diffraction structure determination and analysis at 2.1-2.5 A resolution |
| 2.7.11.24 | purified recombinant His-tagged mutant enzyme in complex with inhibitor furan-2-carboxylic acid (3-[5-(4H-[1,2,4]triazol-3-yl)-1H-indazol-3-yl]-phenyl)-amide in 0.1 M MES, pH5.6, and 0.88 M sodium citrate, mixing of 0.001 ml of protein in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM MgCl2, 5% glycerol, 5 mM DTT, and 0.02% octyl-beta-D-glucopyranoside with 0.001 ml of 0.1 M MES, pH 5.6, 0.56-0.62 M sodium citrate, and 500 nl of 1000fold diluted seed stock, X-ray diffraction structure determination and analysis at 2.15 A resolution, molecular replacment and modelling |
| 2.7.11.24 | purified recombinant p38alpha MAP kinase free or in complex with inhibitor SB203580, sitting or hanging drop vapour diffusion method at 16-20°C, 16 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM MgCl2, 10 mM DTT, and 5% glycerol is mixed with reservoir solution containing 10-20% PEG 4000, 18% ethylene glycol, 0.1 M cacodylic acid, pH 6.0, at a volume ratio of 3:2, X-ray diffraction structure determination and analysis at 1.9-2.7 A resolution |
