ArticleThe Journal of biological chemistry2013
Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
- A Novel SXXLF Motif in the FXR N-Terminal Domain Mediates Coregulator and Interdomain Interactions.Chembiochem : a European journal of chemical biology · 2026Article
- A novel SXXLF motif in the FXR N-terminal domain mediates coregulator and interdomain interactions.bioRxiv : the preprint server for biology · 2026Article
- Structural proteomics defines a sequential priming mechanism for the progesterone receptor.Nature communications · 2025Article
- Article
- International Union of Basic and Clinical Pharmacology CXIII: Nuclear Receptor Superfamily-Update 2023.Pharmacological reviews · 2023Review
- Article
- Identification of ELK1 interacting peptide segments in the androgen receptor.The Biochemical journal · 2022Article
- Activation function 1 of progesterone receptor is required for mammary development and regulation of RANKL during pregnancy.Scientific reports · 2022Article
- Drugging the Undruggable: Targeting the N-Terminal Domain of Nuclear Hormone Receptors.Advances in experimental medicine and biology · 2022Article
- NFAT5, which protects against hypertonicity, is activated by that stress via structuring of its intrinsically disordered domain.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Emerging role of glucocorticoid receptor in castration resistant prostate cancer: A potential therapeutic target.Journal of Cancer · 2020Review
- Role of Phosphorylation in the Modulation of the Glucocorticoid Receptor's Intrinsically Disordered Domain.Biomolecules · 2019Review
- A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain.Structure (London, England : 1993) · 2019Article
- Progesterone Actions During Central Nervous System Development.Frontiers in neuroscience · 2019Review
- Ensemble allosteric model: energetic frustration within the intrinsically disordered glucocorticoid receptor.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Allosteric pathways in nuclear receptors - Potential targets for drug design.Pharmacology & therapeutics · 2018Review
- Site-specific phosphorylation regulates the structure and function of an intrinsically disordered domain of the glucocorticoid receptor.Scientific reports · 2017Article
- DNA-induced unfolding of the thyroid hormone receptor α A/B domain through allostery.FEBS open bio · 2017Article
- Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α.The Journal of biological chemistry · 2015Article
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The N-terminal domain (NTD) of steroid receptors harbors a transcriptional activation function (AF1) that is composed of an intrinsically disordered polypeptide. We examined the interaction of the TATA-binding protein (TBP) with the NTD of the progesterone receptor (PR) and its ability to regulate AF1 activity through coupled folding and binding. As assessed by solution phase biophysical methods, the isolated NTD of PR contains a large content of random coil, and it is capable of adopting secondary α-helical structure and more stable tertiary folding either in the presence of the natural osmolyte trimethylamine-N-oxide or through a direct interaction with TBP. Hydrogen-deuterium exchange coupled with mass spectrometry confirmed the highly dynamic intrinsically disordered property of the NTD within the context of full-length PR. Deletion mapping and point mutagenesis defined a region of the NTD (amino acids 350-428) required for structural folding in response to TBP interaction. Overexpression of TBP in cells enhanced transcriptional activity mediated by the PR NTD, and deletion mutations showed that a region (amino acids 327-428), similar to that required for TBP-induced folding, was required for functional response. TBP also increased steroid receptor co-activator 1 (SRC-1) interaction with the PR NTD and cooperated with SRC-1 to stimulate NTD-dependent transcriptional activity. These data suggest that TBP can mediate structural reorganization of the NTD to facilitate the binding of co-activators required for maximal transcriptional activation.
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