The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding.

@article{Giangrande2000TheOT,
  title={The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding.},
  author={P. Giangrande and Erin A. Kimbrel and Dean P. Edwards and Donald P McDonnell},
  journal={Molecular and cellular biology},
  year={2000},
  volume={20 9},
  pages={3102-15}
}
The human progesterone receptor (PR) exists as two functionally distinct isoforms, hPRA and hPRB. hPRB functions as a transcriptional activator in most cell and promoter contexts, while hPRA is transcriptionally inactive and functions as a strong ligand-dependent transdominant repressor of steroid hormone receptor transcriptional activity. Although the precise mechanism of hPRA-mediated transrepression is not fully understood, an inhibitory domain (ID) within human PR, which is necessary for… CONTINUE READING
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