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Molecular Endocrinology, Vol 7, 1266-1274, Copyright © 1993 by Endocrine Society

ARTICLES

Transcriptional activation by the estrogen receptor requires a conformational change in the ligand binding domain

JM Beekman, GF Allan, SY Tsai, MJ Tsai and BW O'Malley
Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030.

The estrogen receptor (ER) is a strong hormone-inducible transcription factor that regulates the expression of many genes. It was shown for the human progesterone receptor that the binding of hormone causes distinct conformational changes in the ligand binding domain (LBD) and that these changes in LBD conformation are crucial for events after DNA binding. We now show that conformational changes in the LBD of the human ER are a prerequisite for trans-activation. Under the appropriate conditions ER binds to its response element and activates transcription only in the presence of ligand. Binding of the ligand causes changes in the conformation of the LBD. Antihormones induce distinct conformational changes, the differences between the conformations lying in the carboxy-terminal end of the receptor. Changing the experimental conditions results in a receptor that can bind to DNA and activate transcription in a ligand-independent manner. Under these conditions the LBD has a transcriptionally active conformation in the absence of ligand. Taken together, our data indicate that the conformational change induced by ligand is required for converting a receptor to the transcriptionally active form.


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