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• W2056243339 abstract "Estrogen receptors (ERα and ERβ) are ligand-activated transcription factors. We examined the effects of estradiol (E 2 ), 4-hydroxytamoxifen (HT), and the estrogen response element (ERE) on the helical content and thermal unfolding of ERβ. A circular dichroism (CD) spectrum of ERβ showed changes at 210 and 222 nm that were due to the presence of E 2 , which is indicative of partial unfolding. In contrast, HT did not alter the CD spectrum of ERβ. The addition of E 2 + ERE caused an increase in the α-helical content and an increase in the temperature midpoint of folding transition (T M ) from 39 ± 0.7 °C to 57.2 ± 1 °C. The addition of E 2 + mutant ERE, or E 2 + control oligonucleotide, increased the T M of ERβ to 45 ± 2 °C only. In the presence of HT, ERβ yielded similar T M values (55–58 °C) with ERE, mutant ERE, or control oligodeoxynucleotide. The binding affinity of ERβ for ERE increased 125.7-fold as a result of the presence of E 2 , but only 4-fold as a result of HT. These results demonstrate coupled effects of E 2 and ERE on ERβ stability and binding affinity. The increased thermal stability of HT–ERβ–ERE was associated with reduced specificity of ERβ–ERE recognition, illustrating profound differences in conformational states of ERβ induced by E 2 and HT." @default.
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• W2056243339 date "2007-02-01" @default.
• W2056243339 modified "2023-09-25" @default.
• W2056243339 title "Effects of estradiol and 4-hydroxytamoxifen on the conformation, thermal stability, and DNA recognition of estrogen receptor β" @default.
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• W2056243339 doi "https://doi.org/10.1139/o06-144" @default.
• W2056243339 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17464340" @default.
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