Modulation of estrogen receptor alpha function and stability by tamoxifen and a critical amino acid (Asp-538) in helix 12.

@article{Pearce2003ModulationOE,
  title={Modulation of estrogen receptor alpha function and stability by tamoxifen and a critical amino acid (Asp-538) in helix 12.},
  author={Sandra Timm Pearce and Hong Liu and Virgil Craig Jordan},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 9},
  pages={
          7630-8
        }
}
Estrogen receptor alpha (ER) is a ligand-activated transcription factor implicated in breast cancer growth. Selective estrogen receptor modulators (SERMs), such as tamoxifen (4-OHT), bind to the ER and affect the position of helix 12, thereby influencing coregulator binding and ER transcriptional activation. Previous studies have shown that a triple mutation in helix 12 (3m; D538A/E542A/D545A) caused a change in ER stability and obliterated 4-OHT action (Liu, H., Lee, E. S., de los Reyes, A… CONTINUE READING
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