InterPro domain: IPR034335

This entry represents the C-terminal domain of prostaglandin E synthase 2 (also known as membrane-associated prostaglandin E synthase-2, or mPGES2). mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH, or other thiol compounds [ 1 , 2 ]. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature, and mediation of inflammation [ 3 ].

mPGES2 contains an N-terminal hydrophobic domain which is membrane associated and a C-terminal soluble domain with a GST-like structure. The C-terminal GST-like domain contains two structural domains, an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST active site is located in a cleft between the two structural domains.

1. Crystal structure and possible catalytic mechanism of microsomal prostaglandin E synthase type 2 (mPGES-2). J. Mol. Biol. 348, 1163-76
2. Prostaglandin E synthase. Prostaglandins Other Lipid Mediat. 68-69, 383-99
3. Prostaglandin E synthase in the pathophysiology of arthritis. Fundam Clin Pharmacol 19, 255-61