Allosteric modulation of SULT2A1 by celecoxib and nimesulide: computational analyses.
We used protein-ligand docking and minimization to identify celecoxib as an allosteric modulator of SULT2A1-catalyzed estradiol sulfonation. Subsequent to celecoxib docking and complex minimization, conformational changes in SULT2A1 allowed estradiol docking to an alternative binding region with predicted preference for 17beta-OH-E(2) sulfonation over 3-OH-E(2) sulfonation.
Yalcin
Emine Bihter
EB
Department of Biomedical and Pharmaceutical Sciences, College of Pharmacy, University of Rhode Island, Kingston, RI 02881, USA.
Struzik
Scott M
SM
King
Roberta S
RS
D000494:Allosteric Regulation / Q000187:drug effects; D001665:Binding Sites / Q000187:drug effects; D000068579:Celecoxib; D004347:Drug Interactions; D004958:Estradiol / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D011487:Protein Conformation / Q000187:drug effects; D011720:Pyrazoles / Q000494:pharmacology*; D012984:Software; D013449:Sulfonamides / Q000494:pharmacology*; D015238:Sulfotransferases / Q000187:drug effects* / Q000235:genetics
D008024:Ligands; D011720:Pyrazoles; D013449:Sulfonamides; D004958:Estradiol; D015238:Sulfotransferases; C028152:alcohol sulfotransferase; D000068579:Celecoxib; C012655:nimesulide