. . . . . . . . "5486" . "2000-9-27" . . "Prostaglandin H synthase-1 and -2 (PGHS-1 and -2) catalyze the committed step in prostaglandin synthesis and are targets for nonsteroidal anti-inflammatory drugs (NSAIDs) like aspirin. We have determined the structure of PGHS-1 at 3 angstrom resolution with arachidonic acid (AA) bound in a chemically productive conformation. The fatty acid adopts an extended L-shaped conformation that positions the 13proS hydrogen of AA for abstraction by tyrosine-385, the likely radical donor. A space also exists for oxygen addition on the antarafacial surface of the carbon in the 11-position (C-11). While this conformation allows endoperoxide formation between C-11 and C-9, it also implies that a subsequent conformational rearrangement must occur to allow formation of the C-8/C-12 bond and to position C-15 for attack by a second molecule of oxygen." . . . . "eng" . . "IM" . . . . . "MEDLINE" . "Sep" . "0036-8075" . . . . . "Print" . "15" . "289" . "NLM" . "Y" . "1933-7" . "2007-11-14" . . . . . . . . . "2000" . "The productive conformation of arachidonic acid bound to prostaglandin synthase." . "Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824-1319, USA." . "Journal Article" . "Research Support, U.S. Gov't, P.H.S." . "Research Support, U.S. Gov't, Non-P.H.S." .