1diy: Difference between revisions

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{{STRUCTURE_1diy|  PDB=1diy  |  SCENE=  }}  
{{STRUCTURE_1diy|  PDB=1diy  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE CYCLOOXYGENASE ACTIVE SITE OF PGHS-1'''
===CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE CYCLOOXYGENASE ACTIVE SITE OF PGHS-1===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10988074}}


==About this Structure==
==About this Structure==
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[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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