Cloning and Crystal Structure of Hematopoietic Prostaglandin D Synthase

نویسندگان

  • Yoshihide Kanaoka
  • Hideo Ago
  • Eiji Inagaki
  • Toyomichi Nanayama
  • Masashi Miyano
  • Reiko Kikuno
  • Yutaka Fujii
  • Naomi Eguchi
  • Hiroyuki Toh
  • Yoshihiro Urade
  • Osamu Hayaishi
چکیده

Hematopoietic prostaglandin (PG) D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells. We isolated a cDNA for the rat enzyme, crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed with glutathione at 2.3 A resolution. The enzyme is the first member of the sigma class glutathione S-transferase (GST) from vertebrates and possesses a prominent cleft as the active site, which is never seen among other members of the GST family. The unique 3-D architecture of the cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific isomerization from PGH2 to PGD2.

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عنوان ژورنال:
  • Cell

دوره 96  شماره 

صفحات  -

تاریخ انتشار 1997