Stereoselective binding of indomethacin ethanolamide derivatives to cyclooxygenase-1.

Moth CW, Prusakiewicz JJ, Marnett LJ, Lybrand TP
J Med Chem. 2005 48 (10): 3613-20

PMID: 15887968 · DOI:10.1021/jm0494164

We have used molecular modeling studies and molecular dynamics simulations to generate three-dimensional models for cyclooxygenase-1 complexes with a series of indomethacin ethanolamide derivatives. These studies provide a plausible explanation for the stereoselective ligand binding preferences observed experimentally for these inhibitors and predict the general binding mode as well as specific structural details for the ligand-enzyme complexes. These studies provide insight into the nature of cyclooxygenase-1 interactions with a series of novel inhibitors and should help increase our understanding of key structural determinants for cyclooxygenase isozyme-selective inhibitor binding.

MeSH Terms (16)

Animals Binding Sites Cyclooxygenase 1 Cyclooxygenase Inhibitors Ethanolamines Hydrogen Bonding Indomethacin Ligands Models, Molecular Molecular Conformation Prostaglandin-Endoperoxide Synthases Protein Binding Quantitative Structure-Activity Relationship Sheep Stereoisomerism Thermodynamics

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