ArticleProceedings of the National Academy of Sciences of the United States of America2004
TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 85 citations in OpenAlex.
- Selective Modulation of the Human Glucocorticoid Receptor Compromises GR Chromatin Occupancy and Recruitment of p300/CBP and the Mediator Complex.Molecular & cellular proteomics : MCP · 2024Article
- Acetylation-induced proteasomal degradation of the activated glucocorticoid receptor limits hormonal signaling.iScience · 2024Article
- Review
- Drugging the Undruggable: Targeting the N-Terminal Domain of Nuclear Hormone Receptors.Advances in experimental medicine and biology · 2022Article
- Tumor Susceptibility Gene 101 Regulates the Glucocorticoid Receptor through Disorder-Mediated Allostery.Biochemistry · 2021Article
- Bidirectional Crosstalk Between Hypoxia Inducible Factors and Glucocorticoid Signalling in Health and Disease.Frontiers in immunology · 2021Review
- Role of Phosphorylation in the Modulation of the Glucocorticoid Receptor's Intrinsically Disordered Domain.Biomolecules · 2019Review
- A General Introduction to Glucocorticoid Biology.Frontiers in immunology · 2019Review
- Site-specific phosphorylation regulates the structure and function of an intrinsically disordered domain of the glucocorticoid receptor.Scientific reports · 2017Article
- Conditionally disordered proteins: bringing the environment back into the fold.Cellular and molecular life sciences : CMLS · 2017Review
- Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α.The Journal of biological chemistry · 2015Article
- Minireview: dynamic structures of nuclear hormone receptors: new promises and challenges.Molecular endocrinology (Baltimore, Md.) · 2014Review
- Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding.The Journal of biological chemistry · 2013Article
- Determinants of the heightened activity of glucocorticoid receptor translational isoforms.Molecular endocrinology (Baltimore, Md.) · 2013Article
- Nuclear receptors and their selective pharmacologic modulators.Pharmacological reviews · 2013Review
- Binding of the N-terminal region of coactivator TIF2 to the intrinsically disordered AF1 domain of the glucocorticoid receptor is accompanied by conformational reorganizations.The Journal of biological chemistry · 2012Article
- Proinflammatory actions of glucocorticoids: glucocorticoids and TNFα coregulate gene expression in vitro and in vivo.Endocrinology · 2012Article
- Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Endocrine reviews · 2012Review
- Structural and functional analysis of domains of the progesterone receptor.Molecular and cellular endocrinology · 2012Review
- Roles of intrinsic disorder in protein-nucleic acid interactions.Molecular bioSystems · 2012Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
A number of transcription factor proteins contain domains that are fully or partially unstructured. The means by which such proteins acquire naturally folded conformations are not well understood. When they encounter their proper binding partner(s), several of these proteins adopt a folded conformation through an induced-fit mechanism. The glucocorticoid receptor (GR) is a ligand-activated transcription factor. Expressed independently as a recombinant peptide, the N-terminal transactivation domain (AF1) of the GR shows little structure and appears to exist as a collection of random coil configurations. The GR AF1 is known to interact with other transcription factors, including a critical component of the general transcription machinery proteins, the TATA box binding protein (TBP). We tested whether this interaction can lead to acquisition of structure in the GR AF1. Our results show that recombinant GR AF1 acquires a significant amount of helical content when it interacts with TBP. These structural changes were monitored by Fourier transform infrared and NMR spectroscopies, and by proteolytic digestions. Our results support a model in which TBP binding interaction with the GR AF1 induces significantly greater helical structure in the AF1 domain. This increased helical content in the GR AF1 appears to come mostly at the expense of random coil conformation. These results are in accordance with the hypothesis that an induced-fit mechanism gives structure to the GR AF1 when it encounters TBP.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.