Structure of the active site of prostaglandin synthase from studies of depsides: an alternate view.

Abstract

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.

Cite this paper

@article{Gerrard1984StructureOT, title={Structure of the active site of prostaglandin synthase from studies of depsides: an alternate view.}, author={Jonathan M. Gerrard and Douglas A. Peterson}, journal={Prostaglandins, leukotrienes, and medicine}, year={1984}, volume={13 2}, pages={139-42} }