Potent inhibition of human sulfotransferase 1A1 by 17α-ethinylestradiol: role of 3'-phosphoadenosine 5'-phosphosulfate binding and structural rearrangements in regulating inhibition and activity.

@article{Rohn2012PotentIO,
  title={Potent inhibition of human sulfotransferase 1A1 by 17α-ethinylestradiol: role of 3'-phosphoadenosine 5'-phosphosulfate binding and structural rearrangements in regulating inhibition and activity.},
  author={Katie Jo Rohn and Ian Thomas Cook and Thomas S. Leyh and Susan A Kadlubar and Charles N. Falany},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2012},
  volume={40 8},
  pages={
          1588-95
        }
}
Sulfotransferase (SULT) 1A1 is the major drug/xenobiotic-conjugating SULT isoform in human liver because of its broad substrate reactivity and high expression level. SULT1A1 sulfates estrogens with low micromolar K(m) values consistent with its affinity for sulfation of many small phenolic compounds. Binding studies showed the unexpected ability of 17α-ethinylestradiol (EE2) to bind and inhibit SULT1A1 activity toward p-nitrophenol and β-naphthol at low nanomolar concentrations, whereas EE2 was… CONTINUE READING
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Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: a new homology modeling tool

  • MJ Bower, FE Cohen, RL JrDunbrack
  • J Mol Biol
  • 1997
Highly Influential
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