Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains.

@article{Tanenbaum1998CrystallographicCO,
  title={Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains.},
  author={D M Tanenbaum and Yong Wang and Shawn P. Williams and Paul B. Sigler},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 11},
  pages={5998-6003}
}
The 2.8-A crystal structure of the complex formed by estradiol and the human estrogen receptor-alpha ligand binding domain (hERalphaLBD) is described and compared with the recently reported structure of the progesterone complex of the human progesterone receptor ligand binding domain, as well as with similar structures of steroid/nuclear receptor LBDs solved elsewhere. The hormone-bound hERalphaLBD forms a distinctly different and probably more physiologically important dimer interface than its… CONTINUE READING
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Tanenbaum et al

  • E. M. McInerney, B. A. Ince, D. J. Shapiro, Katzenellenbogen, 10 B.S.Mol.Endocrinol., 1519–1526. Biochemistry
  • Proc. Natl. Acad. Sci. USA 95
  • 1998
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