NMR resonance assignments of mouse lipocalin-type prostaglandin D synthase/prostaglandin J complex

Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) catalyzes the isomerization of PGH to produce PGD, an endogenous somenogen, in the brains of various mammalians. We recently reported that various other PGs also bind to L-PGDS, suggesting that it could serve as an extracellular carrier for PGs. Although the solution and crystal structure of L-PGDS has been determined, as has the structure of L-PGDS complexed PGH analog, a structural analysis of L-PGDS complexed with other PGs is needed in order to understand the mechanism responsible for the PG trapping. Here, we report the nearly complete H, C, and N backbone and side chain resonance assignments of the L-PGDS/PGJ complex and the binding site for PGJ on L-PGDS.