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- W2059613886 abstract "Lipocalin-type Prostaglandin D synthase (L-PGDS) catalyzes the isomerization of prostaglandin H2 (PGH2) to produce prostaglandin D2 (PGD2), which acts as a somnogen in the brain. This enzyme belongs to the lipocalin superfamily which consists of transporter proteins for lipophilic substances in the extracellular space. Our previous studies suggested that L-PGDS is comprised of a β-barrel structure with a hydrophobic pocket and the active thiol group of Cys65 is located in this pocket and faces the inside of the pocket. A number of studies of L-PGDS, as a drug target for treating sleep disorders, have been reported, in attempts to understand its catalytic mechanism, and several substrate recognition models of L-PGDS have been proposed. However, details of the mechanism by which L-PDGS recognizes its substrates and products are obscure, since essential information, such as its binding affinity and stoichiometry of the interactions between L-PGDS and its substrate and product remains unclear. To address this, the binding properties of the molecule were examined by isothermal titration calorimetry (ITC) and NMR experiments. The results of the ITC measurements revealed that, not only the substrate analog, but also the product bind to L-PGDS in a stoichiometry of 2 to 1 and that L-PGDS possesses two binding sites (high and low affinity sites). In addition, NMR titration and ITC experiments of L-PGDS mutants indicated that the active Cys65 residue is located at the high affinity-binding site and plays a critical role in the binding of the substrate and product to L-PGDS." @default.
- W2059613886 created "2016-06-24" @default.
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- W2059613886 date "2015-01-01" @default.
- W2059613886 modified "2023-09-28" @default.
- W2059613886 title "The Interaction between L-PGDS and its Substrates or Products, as Determined by Isothermal Titration Calorimetry and NMR" @default.
- W2059613886 doi "https://doi.org/10.1016/j.bpj.2014.11.2813" @default.
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