ArticleBiochemistry2016
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Autoinhibition of untimely DNA binding by structural disorder in the full-length peroxisome proliferator-activated receptors (PPARs).Nature communications · 2026Article
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- A Novel Mechanism of Coactivator Recruitment by the Nurr1 Nuclear Receptor.Journal of molecular biology · 2022Article
- Review
- Structural basis for DNA recognition and allosteric control of the retinoic acid receptors RAR-RXR.Nucleic acids research · 2020Article
- RXRα Positively Regulates Expression of the ChickenFrontiers in cell and developmental biology · 2020Article
- A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain.Structure (London, England : 1993) · 2019Article
- Protein-nucleic acids interactions: new ways of connecting structure, dynamics and function.Biophysical reviews · 2017Article
- Structure of the homodimeric androgen receptor ligand-binding domain.Nature communications · 2017Article
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Authors and funding
7 authors.
Funding
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Abstract
Retinoid X receptors (RXRs) are transcription factors with important functions in embryonic development, metabolic processes, differentiation, and apoptosis. A particular feature of RXRs is their ability to act as obligatory heterodimerization partners of class II nuclear receptors. At the same time, these receptors are also able to form homodimers that bind to direct repeat separated by one nucleotide hormone response elements. Since the discovery of RXRs, most of the studies focused on its ligand binding and DNA binding domains, while its N-terminal domain (NTD) harboring a ligand-independent activation function remained poorly characterized. Here, we investigated the solution properties of the NTD of RXRα alone and in the context of the full-length receptor using small-angle X-ray scattering and nuclear magnetic resonance spectroscopy. We report the solution structure of the full-length homodimeric RXRα on DNA and show that the NTD remains highly flexible within this complex.
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