Structure of the active site of prostaglandin synthase from studies of depsides: an alternate view.
Evaluation of the structure of the lichen depside, 4-0-methylcryptochlorophaeic acid, the most potent inhibitor of prostaglandin synthesis known, and its potential interaction with heme supports a model of the active site of prostaglandin synthase initially suggested by studies of arachidonic acid-heme interaction.
D001665:Binding Sites; D016861:Cyclooxygenase Inhibitors; D053630:Depsides; D006418:Heme; D062385:Hydroxybenzoates / Q000494:pharmacology*; D008958:Models, Molecular; D013329:Structure-Activity Relationship
D016861:Cyclooxygenase Inhibitors; D053630:Depsides; D062385:Hydroxybenzoates; D006418:Heme