Open AccessHigh‐quality crystals of human haematopoietic prostaglandin D synthase with novel inhibitors
Author(s) -
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
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110020828
Subject(s) - haematopoiesis , prostaglandin d2 , atp synthase , prostaglandin , chemistry , synchrotron radiation , microbiology and biotechnology , enzyme , biology , biochemistry , physics , optics , stem cell
Human haematopoietic prostaglandin D synthase (H‐PGDS; EC 5.3.99.2) produces prostaglandin D 2 , an allergic and inflammatory mediator, in mast cells and Th2 cells. H‐PGDS has been crystallized with novel inhibitors with half‐maximal inhibitory concentrations (IC 50 ) 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 IC 50 value of 50 n M 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.