ArticleNucleic acids research2007
Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domain.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 43 citations in OpenAlex.
- Nuclear receptors in health and disease: signaling pathways, biological functions and pharmaceutical interventions.Signal transduction and targeted therapy · 2025Review
- RNA fine-tunes estrogen receptor-alpha binding on low-affinity DNA motifs for transcriptional regulation.The EMBO journal · 2024Article
- Conformation-dependent restraints for polynucleotides: the sugar moiety.Nucleic acids research · 2020Article
- Conformation-dependent restraints for polynucleotides: I. Clustering of the geometry of the phosphodiester group.Nucleic acids research · 2016Article
- Relationship of structure and function of DNA-binding domain in vitamin D receptor.Molecules (Basel, Switzerland) · 2015Review
- Structural basis of natural promoter recognition by the retinoid X nuclear receptor.Scientific reports · 2015Article
- Article
- The retinoid X receptors and their ligands.Biochimica et biophysica acta · 2012Review
- Dual FRET assay for detecting receptor protein interaction with DNA.Nucleic acids research · 2010Article
- Ecdysteroid hormone action.Cellular and molecular life sciences : CMLS · 2009Review
- Structural basis of natural promoter recognition by a unique nuclear receptor, HNF4alpha. Diabetes gene product.The Journal of biological chemistry · 2008Article
- Equilibrium analysis of the DNA binding domain of the ultraspiracle protein interaction with the response element from the hsp27 gene promoter--the application of molecular beacon technology.Journal of fluorescence · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heterodimer of the ecdysone receptor (EcR) and ultraspiracle (Usp), members of the nuclear receptors superfamily, is considered as the functional receptor for ecdysteroids initiating molting and metamorphosis in insects. Here we report the 1.95 A structure of the complex formed by the DNA-binding domains (DBDs) the EcR and the Usp, bound to the natural pseudopalindromic response element. Comparison of the structure with that obtained previously, using an idealized response element, shows how the EcRDBD, which has been previously reported to possess extraordinary flexibility, accommodates DNA-induced structural changes. Part of the C-terminal extension (CTE) of the EcRDBD folds into an alpha-helix whose location in the minor groove does not match any of the locations previously observed for nuclear receptors. Mutational analyses suggest that the alpha-helix is a component of EcR-box, a novel element indispensable for DNA-binding and located within the nuclear receptor CTE. This element seems to be a general feature of all known EcRs.
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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.