ArticleBiophysical chemistry2013
Analysis of a glucocorticoid-estrogen receptor chimera reveals that dimerization energetics are under ionic control.
Article in Biophysical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- A Mechanistic High-Content Analysis Assay Using a Chimeric Androgen Receptor That Rapidly Characterizes Androgenic Chemicals.SLAS discovery : advancing life sciences R & D · 2020Article
- Using Evolution to Guide Protein Engineering: The Devil IS in the Details.Biophysical journal · 2016Review
- Differential Regulation of Progesterone Receptor-Mediated Transcription by CDK2 and DNA-PK.Molecular endocrinology (Baltimore, Md.) · 2016Article
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5 authors.
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Abstract
Steroid receptors assemble at DNA response elements as dimers, resulting in coactivator recruitment and transcriptional activation. Our work has focused on dissecting the energetics associated with these events and quantitatively correlating the results with function. A recent finding is that different receptors dimerize with large differences in energetics. For example, estrogen receptor-α (ER-α) dimerizes with a ΔG=-12.0 kcal/mol under conditions in which the glucocorticoid receptor (GR) dimerizes with a ΔG≤-5.1 kcal/mol. To determine the molecular forces responsible for such differences, we created a GR/ER chimera, replacing the hormone-binding domain (HBD) of GR with that of ER-α. Cellular and biophysical analyses demonstrate that the chimera is functionally active. However, GR/ER dimerization energetics are intermediate between the parent proteins and coupled to a strong ionic linkage. Since the ER-α HBD is the primary contributor to dimerization, we suggest that GR residues constrain an ion-regulated HBD assembly reaction.
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