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X-Ray Crystallographic Study of the Structure of Prostaglandin H Synthase
Book chapter   Peer reviewed

X-Ray Crystallographic Study of the Structure of Prostaglandin H Synthase

Daniel Picot, Patrick J. Loll and R. Michael Garavito
Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury 2, pp 107-111
1997
PMID: 9547544

Abstract

Acetyl Salicylate Amphipathic Helix Arachidonate Cascade Cyclooxygenase Reaction Subunit Interface
Prostaglandin H synthase (PGHS) is the first enzyme in the prostaglandin pathway of the arachidonate cascade (1). It is a bifunctional enzyme that catalyzes the conversion of arachidonic acid into prostaglandin H2 (PGH2). Two isozymes of the enzyme (PGHS-1 and PGHS-2) exist and have different modes of expression and tissue distributions (2). The first reaction catalyzed by PGHS, the cyclooxygenase step (3), inserts two molecules of oxygen into arachidonic acid to produce prostaglandin G2 (PGG2). In the second step, the peroxidase reaction reduces the hydroperoxide PGG2 to PGH2. PGHS, a high-spin ferric heme protein with molecular weight of 70 kDa per subunit (3), can form a dimer in solution, but its physiological aggregation state is uncertain. While PGHS is an integral membrane protein, found mainly in the endoplasmic reticulum, its mode of insertion into biological membranes was unknown until recently. In this communication, we described the structure of ovine PGHS-1, recently determined by X-ray crystallography at 3.5 Å (4) using crystals grown in the presence of detergents (5).

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Web of Science research areas
Medicine, Research & Experimental
Oncology
Radiology, Nuclear Medicine & Medical Imaging
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