2Y0J

Triazoloquinazolines as a novel class of phosphodiesterase 10A (PDE10A) inhibitors, part 2, Lead-optimisation.

Summary for 2Y0J

• Entry DOI: 10.2210/pdb2y0j/pdb
• Related: 1LRB 2WEY
• Descriptor: CAMP AND CAMP-INHIBITED CGMP 3', 5'-CYCLIC PHOSPHODIESTERASE 10A, 5-(1H-BENZIMIDAZOL-2-YLMETHYLSULFANYL)-2-METHYL-[1,2,4]TRIAZOLO[1,5-C]QUINAZOLINE, ZINC ION, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: Q9Y233
• Total number of polymer chains: 2
• Total formula weight: 80125.31

Authors

Kehler, J.,Ritzen, A.,Langgard, M.,Petersen, S.L.,Christoffersen, C.T.,Nielsen, J.,Kilburn, J.P. (deposition date: 2010-12-03, release date: 2011-06-15, Last modification date: 2023-12-20)

Primary citation

Kehler, J.,Ritzen, A.,Langgard, M.,Petersen, S.L.,Farah, M.M.,Bundgaard, C.,Christoffersen, C.T.,Nielsen, J.,Kilburn, J.P.
Triazoloquinazolines as a Novel Class of Phosphodiesterase 10A (Pde10A) Inhibitors.
Bioorg.Med.Chem.Lett., 21:3738-, 2011

PubMed Abstract: Novel triazoloquinazolines have been found as phosphodiesterase 10A (PDE10A) inhibitors. Structure-activity studies improved the initial micromolar potency which was found in the lead compound by a 100-fold identifying 5-(1H-benzoimidazol-2-ylmethylsulfanyl)-2-methyl-[1,2,4]triazolo[1,5-c]quinazoline, 42 (PDE10A IC(50)=12 nM) as the most potent compound from the series. Two X-ray structures revealed novel binding modes to the catalytic site of the PDE10A enzyme.

PubMed: 21602043
DOI: 10.1016/J.BMCL.2011.04.067

Experimental method

X-RAY DIFFRACTION (2.43 Å)