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Results 1 - 3 of 3
EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.12.1purified enzyme DYRK1A bound to inhibitor midostaurin, sitting drop vapour diffusion method, mixing of 200 nl of 7-10 mg/ml protein in 50 mM MOPS, pH 6.8, 50 mM KCl, 2 mM 2-mercaptoethanol, with 200 nl of precipitant solution containing 10-16% PEG 3350, 0.1 M potassium thiocyanate, 0.1 M KCl (or 0.1 M NaCl or 0.1 M LiCl), for co-crystallization with the inhibitor midostaurin, protein is mixed in a 1:1 ratio with the inhibitor in crystallization solution, containing 100 mM potassium thiocyanate, 50-100 mM LiCl (or NaCl or KCl), and 10-16% PEG 3350, to give a final drop size of 0.004 ml, by hanging drop vapour diffusion method, 5-7 days at room temperature, X-ray diffraction structure determination and analysis at 2.6 A resolution 739790
Display the word mapDisplay the reaction diagram Show all sequences 2.7.12.1purified enzyme DYRK1B bound to inhibitor midostaurin, X-ray diffraction structure determination and analysis 739790
Display the word mapDisplay the reaction diagram Show all sequences 2.7.12.1structure of the mature form in complex with inhibitor harmine, to 1.9 A resolution. The phosphorylation of residue S350 increases the stability of DYRK3 and enhances its kinase activity. The N-terminal autophosphorylation accessory domain stabilizes the DYRK3 protein, followed by autophosphorylation of the tyrosine of the activation loop, which is important for kinase activity 761697
Results 1 - 3 of 3