Modeling Cyclooxygenase Inhibition. Implication of Active Site Hydration on the Selectivity of Ketoprofen Analogues
Journal of Medicinal Chemistry2000Vol. 43(11), pp. 2280–2284
Citations Over TimeTop 13% of 2000 papers
Albert Palomer, Juan J. Pérez, Susana Navea, Oriol Llorens, Jaume Pascual, Lluïsa García, David Mauleón
Abstract
Molecular modeling studies performed on the two cyclooxygenase isozymes (COXs) suggest that active site hydration is crucial for understanding inhibitor selectivity. In this work, models have been constructed considering some implicit water molecules, placed in the position suggested by GRID, that participate in the dynamic hydrogen-bonding network at the polar active site entrance together with protein residues 355, 524, 120, and 513. The selectivity observed for ketoprofen (1) and the structural analogues 2 and 3 may be rationalized in terms of such implicit hydration.
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