High-quality crystals of human haematopoietic prostaglandin D synthase with novel inhibitors

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-06, Vol.66 (7), p.846-850
• Main Authors: Takahashi, Sachiko, Tsurumura, Toshiharu, Aritake, Kosuke, Furubayashi, Naoki, Sato, Masaru, Yamanaka, Mari, Hirota, Erika, Sano, Satoshi, Kobayashi, Tomoyuki, Tanaka, Tetsuo, Inaka, Koji, Tanaka, Hiroaki, Urade, Yoshihiro
• Format: Article
• Language: English
• Subjects: allergy; Crystallization; Crystallization Communications; Crystallography, X-Ray; Crystals; Enzyme Inhibitors - chemistry; Human; human haematopoietic prostaglandin D synthase; Humans; inflammatory reaction; Inhibitors; Intramolecular Oxidoreductases - antagonists & inhibitors; Intramolecular Oxidoreductases - chemistry; Lipocalins - antagonists & inhibitors; Lipocalins - chemistry; microgravity; Nanocomposites; Nanomaterials; Nanostructure; prostaglandin D2; Prostaglandins; Service Module (ISS); X-ray diffraction
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S1744309110020828

Human haematopoietic prostaglandin D synthase (H‐PGDS; EC 5.3.99.2) produces prostaglandin D2, an allergic and inflammatory mediator, in mast cells and Th2 cells. H‐PGDS has been crystallized with novel inhibitors with half‐maximal inhibitory concentrations (IC50) in the low nanomolar range by the counter‐diffusion method onboard the Russian Service Module on the International Space Station. The X‐ray diffraction of a microgravity‐grown crystal of H‐PGDS complexed with an inhibitor with an IC50 value of 50 nM extended to 1.1 Å resolution at 100 K using SPring‐8 synchrotron radiation, which is one of the highest resolutions obtained to date for this protein.