ArticleThe Journal of biological chemistry2011
Structural basis for retinoic X receptor repression on the tetramer.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 47 citations in OpenAlex.
- Retinoid-X receptor action and disruption in development.Developmental biology · 2026Review
- Anabolic-Androgenic Steroids Revisited: Structural Biology, Receptor Signaling, and Mechanisms of Anabolic-Androgenic Dissociation.International journal of molecular sciences · 2026Review
- Simple Fluorescence Labeling Method Enables Detection of Intracellular Distribution and Expression Level of Retinoid X Receptors.ACS medicinal chemistry letters · 2024Article
- Article
- A molecular switch regulating transcriptional repression and activation of PPARγ.Nature communications · 2020Article
- Protein profiling of SH-SY5Y neuroblastoma cells: The effect of rhein.Journal of biosciences · 2019Article
- Glucocorticoid receptor quaternary structure drives chromatin occupancy and transcriptional outcome.Genome research · 2019Article
- A revisited version of the apo structure of the ligand-binding domain of the human nuclear receptor retinoic X receptor α.Acta crystallographica. Section F, Structural biology communications · 2019Article
- An integrated strategy for identifying new targets and inferring the mechanism of action: taking rhein as an example.BMC bioinformatics · 2018Article
- Retinoid X Receptor Antagonists.International journal of molecular sciences · 2018Review
- Benzophenone-3 Impairs Autophagy, Alters Epigenetic Status, and Disrupts Retinoid X Receptor Signaling in Apoptotic Neuronal Cells.Molecular neurobiology · 2018Article
- Antagonist-perturbation mechanism for activation function-2 fixed motifs: active conformation and docking mode of retinoid X receptor antagonists.Journal of computer-aided molecular design · 2017Article
- The Crucial Involvement of Retinoid X Receptors in DDE Neurotoxicity.Neurotoxicity research · 2016Article
- Targeting truncated RXRα for cancer therapy.Acta biochimica et biophysica Sinica · 2016Review
- Structural Basis for Small Molecule NDB (N-Benzyl-N-(3-(tert-butyl)-4-hydroxyphenyl)-2,6-dichloro-4-(dimethylamino) Benzamide) as a Selective Antagonist of Farnesoid X Receptor α (FXRα) in Stabilizing the Homodimerization of the Receptor.The Journal of biological chemistry · 2015Article
- Regulation of the nongenomic actions of retinoid X receptor-α by targeting the coregulator-binding sites.Acta pharmacologica Sinica · 2015Review
- Targeting nuclear receptors with marine natural products.Marine drugs · 2014Review
- Defining the communication between agonist and coactivator binding in the retinoid X receptor α ligand binding domain.The Journal of biological chemistry · 2014Article
- Retinoic acid actions through mammalian nuclear receptors.Chemical reviews · 2014Review
- Synthesis and SAR study of modulators inhibiting tRXRα-dependent AKT activation.European journal of medicinal chemistry · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Retinoic X receptor (RXR) is a master nuclear receptor in the processes of cell development and homeostasis. Unliganded RXR exists in an autorepressed tetramer, and agonists can induce RXR dimerization and coactivator recruitment for activation. However, the molecular mechanisms involving the corepressor recruitment and antagonist-mediated repression of RXR are still elusive. Here we report the crystal structure of RXRα ligand-binding domain (LBD) complexed with silencing mediator for retinoid and thyroid hormone receptors (SMRT) corepressor motif. As the first structural report on the unliganded nuclear receptor bound to the corepressor motif, RXRαLBD-SMRT exhibits a significant structural rearrangement, compared with apoRXRαLBD tetramer. To elucidate further the molecular determinants for RXR repression by its antagonist, we also determine the crystal structure of RXRαLBD-SMRT complexed with the identified antagonist rhein. In the structure, two rhein molecules and two SMRT peptides are in the RXRαLBD tetramer, different from the case in RXRαLBD-SMRT structure, where four SMRT peptides bind to RXRαLBD tetramer. It seems that rhein induces a displacement of SMRT motif by activation function 2 (AF-2) motif binding to the receptor. Combining our current work with the published results, structural superposition of RXRαLBDs in different states reveals that RXR uses an overlapped binding site for coactivator, corepressor, and AF-2 motifs, whereas the AF-2 motif adopts different conformations for agonist or antagonist interaction and coactivator or corepressor recruitment. Taken together, we thus propose a molecular model of RXR repression on the tetramer.
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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.