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Related Experiment Videos

Atomic structure of progesterone complexed with its receptor

S P Williams1, P B Sigler

  • 1Department of Molecular Biophysics and Biochemistry, and the Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510, USA.

Nature
|June 10, 1998
PubMed
Summary

We determined the crystal structure of the human progesterone receptor bound to progesterone. This reveals how the receptor recognizes progestins and forms dimers, offering insights into birth control mechanisms.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Progestins exert physiological effects via the progesterone receptor, a nuclear receptor crucial for pregnancy maintenance.
  • The progesterone receptor is a key pharmaceutical target due to its role in reproductive health.

Purpose of the Study:

  • To elucidate the 1.8 Å crystal structure of the human progesterone receptor's ligand-binding domain complexed with progesterone.
  • To understand the structural basis for selective progestin binding and receptor dimerization.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structure.
  • Biochemical assays were used to assess ligand-dependent protease resistance and repression.

Main Results:

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  • The structure reveals a unique dimerization mode distinct from related nuclear receptors.
  • Hormone-induced stabilization of the ligand-binding domain's C-terminal structure dictates dimer stereochemistry.
  • This stabilization explains ligand-dependent protease resistance, loss of repression, and the mechanism of anti-progestin action.

Conclusions:

  • The determined structure provides a molecular understanding of progestin recognition and progesterone receptor activation.
  • The findings offer insights into the mechanism of action for contraceptives like RU486.
  • This structural model may apply to other 3-keto-steroid receptors, suggesting conserved mechanisms.