1pd2
From Proteopedia
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[[Image:1pd2.gif|left|200px]] | [[Image:1pd2.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE''' | '''CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE''' | ||
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[[Category: Ago, H.]] | [[Category: Ago, H.]] | ||
[[Category: Miyano, M.]] | [[Category: Miyano, M.]] | ||
- | [[Category: | + | [[Category: Gst]] |
- | [[Category: | + | [[Category: Hematopoietic prostaglandin d synthase]] |
- | [[Category: | + | [[Category: Pgd]] |
- | [[Category: | + | [[Category: Sigma-class gst]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:57:14 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 01:57, 3 May 2008
CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE
Overview
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.
About this Structure
1PD2 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Cloning and crystal structure of hematopoietic prostaglandin D synthase., Kanaoka Y, Ago H, Inagaki E, Nanayama T, Miyano M, Kikuno R, Fujii Y, Eguchi N, Toh H, Urade Y, Hayaishi O, Cell. 1997 Sep 19;90(6):1085-95. PMID:9323136 Page seeded by OCA on Sat May 3 04:57:14 2008