Crystal Structures of mPGES-1 Inhibitor Complexes Form a Basis for the Rational Design of Potent Analgesic and Anti-Inflammatory Therapeutics [electronic resource]

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Tác giả:

Ngôn ngữ: eng

Ký hiệu phân loại: 572.4 *Metabolism

Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2015

Mô tả vật lý: Size: p. 4727-4737 : , digital, PDF file.

Bộ sưu tập: Metadata

ID: 261179

 Microsomal prostaglandin E synthase 1 (mPGES-1) is an ?-helical homotrimeric integral membrane inducible enzyme that catalyzes the formation of prostaglandin E<
 sub>
 2<
 /sub>
  (PGE<
 sub>
 2<
 /sub>
 ) from prostaglandin H<
 sub>
 2<
 /sub>
  (PGH<
 sub>
 2<
 /sub>
 ). Inhibition of mPGES-1 has been proposed as a therapeutic strategy for the treatment of pain, inflammation, and some cancers. Interest in mPGES-1 inhibition can, in part, be attributed to the potential circumvention of cardiovascular risks associated with anti-inflammatory cyclooxygenase 2 inhibitors (coxibs) by targeting the prostaglandin pathway downstream of PGH<
 sub>
 2<
 /sub>
  synthesis and avoiding suppression of antithrombotic prostacyclin production. In this work, we determined the crystal structure of mPGES-1 bound to four potent inhibitors in order to understand their structure?activity relationships and provide a framework for the rational design of improved molecules. In addition, we developed a light-scattering-based thermal stability assay to identify molecules for crystallographic studies.
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