A Novel Mechanism of Cyclooxygenase-2 Inhibition Involving Interactions with Ser-530 and Tyr-385*

@article{Rowlinson2003ANM,
  title={A Novel Mechanism of Cyclooxygenase-2 Inhibition Involving Interactions with Ser-530 and Tyr-385*},
  author={Scott W. Rowlinson and James R. Kiefer and Jeffery J. Prusakiewicz and Jennifer L. Pawlitz and Kevin R. Kozak and Amit S. Kalgutkar and William C. Stallings and Ravi G. Kurumbail and Lawrence J. Marnett},
  journal={Journal of Biological Chemistry},
  year={2003},
  volume={278},
  pages={45763 - 45769}
}
A variety of drugs inhibit the conversion of arachidonic acid to prostaglandin G2 by the cyclooxygenase (COX) activity of prostaglandin endoperoxide synthases. Several modes of inhibitor binding in the COX active site have been described including ion pairing of carboxylic acid containing inhibitors with Arg-120 of COX-1 and COX-2 and insertion of arylsulfonamides and sulfones into the COX-2 side pocket. Recent crystallographic evidence suggests that Tyr-385 and Ser-530 chelate polar or… Expand
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TLDR
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TLDR
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