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Results 1 - 10 of 10
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53catalytic domain of inactive mutant D201N in complex with substrate cAMP at 1.56 A resolution. Q369 forms only one hydrogen bond ith the adenine of cAMP. Structural comparison between isoform PDE4D2-cAMP and PDE10A2-cAMP shows an anti configuration of cAMP in PDE4, but syn in PDE10
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53hanging drop method, PDE4D2 in complex with the nonselective inhibitor 3-isobutyl-1-methylxanthine
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53hanging-drop vapor-diffusion method, crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP (2.0 A), 8-Br-AMP (2.13 A), and rolipram (2.0 A)
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53in complex with inhibitor 4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid, comparison with isoforms PDE4A, PDE4B, PDE4C. Inhibitor binds in the same conformation to the deep cAMP substrate pocket and interacts with the same residues in each instance. Detailed structural comparison
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53in complex with inhibitor 4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid, comparison with isoforms PDE4A, PDE4C, PDE4D. Inhibitor binds in the same conformation to the deep cAMP substrate pocket and interacts with the same resiudues in each instance. Detailed structural comparison
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53in complex with inhibitor 4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid, comparison with isoforms PDE4B, PDE4C, PDE4D. Inhibitor binds in the same conformation to the deep cAMP substrate pocket and interacts with the same residues in each instance. Detailed structural comparison
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53molecular dynamics simulations. The second bridging ligand in the active site is HO- rather than H2O, serving as a nucleophile to initialize the catalytic hydrolysis of cAMP
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53NMR and CD analysis of the N-terminal 38mer peptide of isoform PDE4D5 which contains the entire signaling scaffold protein RACK1 interaction domain together with a portion of the beta-arrestin binding site. The peptiode has a distinct amphipathic helical structure. Study on binding to RACK1 and to beta-arrestin
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53unliganded PDE8A1 and in complex with 3-isobuytl-1-methylxanthine, hanging drop vapour diffusion method, using 100 mM sodium cacodylate (pH 6.5), 15% 2-propanol, 30% ethylene glycol, and 8-10% PEG3350 at 4°C
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.53unliganded, detailed structural comparison with isoforms PDE4A, PDE4B, PDE4C
Results 1 - 10 of 10