ArticleThe EMBO journal2003
Structure of the heterodimeric ecdysone receptor DNA-binding complex.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed.
- Epigenetic regulation and posttranslational modifications of FXR: underlying mechanisms and implications in digestive diseases.Acta pharmacologica Sinica · 2026Review
- Molecular Characterization and Expression of the Ecdysone Receptor and Ultraspiracle Genes in the Wheat Blossom Midge,Insects · 2025Article
- Simulations Reveal Unique Roles for the FXR Hinge in the FXR-RXR Nuclear Receptor Heterodimer.ACS bio & med chem Au · 2025Article
- Structures of human TR4LBD-JAZF1 and TR4DBD-DNA complexes reveal the molecular basis of transcriptional regulation.Nucleic acids research · 2023Article
- Molecular interplay between ecdysone receptor and retinoid X receptor in regulating the molting of the Chinese mitten crab,Frontiers in endocrinology · 2023Article
- Structural basis of the farnesoid X receptor/retinoid X receptor heterodimer on inverted repeat DNA.Computational and structural biotechnology journal · 2023Article
- Retinoic acid receptor structures: the journey from single domains to full-length complex.Journal of molecular endocrinology · 2022Article
- Cross-talk of insulin-like peptides, juvenile hormone, and 20-hydroxyecdysone in regulation of metabolism in the mosquitoProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Rapid Assessment of Insect Steroid Hormone Entry Into Cultured Cells.Frontiers in physiology · 2021Article
- Post-Translational Modifications of FXR; Implications for Cholestasis and Obesity-Related Disorders.Frontiers in endocrinology · 2021Review
- Farnesoid X receptor (FXR): Structures and ligands.Computational and structural biotechnology journal · 2021Review
- Mode of Action of Farnesol, the "Noble Unknown" in Particular in CaFrontiers in neuroscience · 2019Article
- Identification of target genes for RNAi-mediated control of the Twospotted Spider Mite.Scientific reports · 2018Article
- Mutations in the nuclear bile acid receptor FXR cause progressive familial intrahepatic cholestasis.Nature communications · 2016Article
- Characterization of a novel RXR receptor in the salmon louse (Lepeophtheirus salmonis, Copepoda) regulating growth and female reproduction.BMC genomics · 2015Article
- Phospholipase Cγ1 connects the cell membrane pathway to the nuclear receptor pathway in insect steroid hormone signaling.The Journal of biological chemistry · 2014Article
- Retinoic acid actions through mammalian nuclear receptors.Chemical reviews · 2014Review
- Article
- Understanding nuclear receptor form and function using structural biology.Journal of molecular endocrinology · 2013Review
- Retinoic acid receptors recognize the mouse genome through binding elements with diverse spacing and topology.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Ecdysteroids initiate molting and metamorphosis in insects via a heterodimeric receptor consisting of the ecdysone receptor (EcR) and ultraspiracle (USP). The EcR-USP heterodimer preferentially mediates transcription through highly degenerate pseudo-palindromic response elements, resembling inverted repeats of 5'-AGGTCA-3' separated by 1 bp (IR-1). The requirement for a heterodimeric arrangement of EcR-USP subunits to bind to a symmetric DNA is unusual within the nuclear receptor superfamily. We describe the 2.24 A structure of the EcR-USP DNA-binding domain (DBD) heterodimer bound to an idealized IR-1 element. EcR and USP use similar surfaces, and rely on the deformed minor groove of the DNA to establish protein-protein contacts. As retinoid X receptor (RXR) is the mammalian homolog of USP, we also solved the 2.60 A crystal structure of the EcR-RXR DBD heterodimer on IR-1 and found the dimerization and DNA-binding interfaces to be the same as in the EcR-USP complex. Sequence alignments indicate that the EcR-RXR heterodimer is an important model for understanding how the FXR-RXR heterodimer binds to IR-1 sites.
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Registered trials
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