ArticleMolecular and cellular biology2012
Evidence for DNA-binding domain--ligand-binding domain communications in the androgen receptor.
Article in Molecular and cellular biology, 2012. 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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Who cites it
31 citing papers in PubMed, 60 citations in OpenAlex.
- Autoinhibition of untimely DNA binding by structural disorder in the full-length peroxisome proliferator-activated receptors (PPARs).Nature communications · 2026Article
- Genome-wide analysis reveals ligand-dependent allostery in RARα:RXR-mediated transcriptional regulation.Cell reports · 2026Article
- Genomic Crosstalk Between Nuclear Receptors in Hormone-dependent Cancers.Endocrinology · 2025Review
- Article
- The Integration of Metabolomics with Other Omics: Insights into Understanding Prostate Cancer.Metabolites · 2022Review
- The androgen receptor depends on ligand-binding domain dimerization for transcriptional activation.EMBO reports · 2021Article
- Evolution of Hominin Detoxification: Neanderthal and Modern Human Ah Receptor Respond Similarly to TCDD.Molecular biology and evolution · 2021Article
- Molecular Dynamics Simulations of a Chimeric Androgen Receptor Protein (SPARKI) Confirm the Importance of the Dimerization Domain on DNA Binding Specificity.Frontiers in molecular biosciences · 2020Article
- Ligand induced dissociation of the AR homodimer precedes AR monomer translocation to the nucleus.Scientific reports · 2019Article
- Molecular Mechanisms and Therapeutics for SBMA/Kennedy's Disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2019Review
- Allosteric pathways in nuclear receptors - Potential targets for drug design.Pharmacology & therapeutics · 2018Review
- DNA-induced unfolding of the thyroid hormone receptor α A/B domain through allostery.FEBS open bio · 2017Article
- Comparing the rules of engagement of androgen and glucocorticoid receptors.Cellular and molecular life sciences : CMLS · 2017Review
- Article
- Structure of the homodimeric androgen receptor ligand-binding domain.Nature communications · 2017Article
- ERG signaling in prostate cancer is driven through PRMT5-dependent methylation of the Androgen Receptor.eLife · 2016Article
- Targeting chromatin binding regulation of constitutively active AR variants to overcome prostate cancer resistance to endocrine-based therapies.Nucleic acids research · 2015Article
- Agonist and antagonist switch DNA motifs recognized by human androgen receptor in prostate cancer.The EMBO journal · 2015Article
- Androgen receptor: structure, role in prostate cancer and drug discovery.Acta pharmacologica Sinica · 2015Review
- Nuclear receptor full-length architectures: confronting myth and illusion with high resolution.Trends in biochemical sciences · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA binding as well as ligand binding by nuclear receptors has been studied extensively. Both binding functions are attributed to isolated domains of which the structure is known. The crystal structure of a complete receptor in complex with its ligand and DNA-response element, however, has been solved only for the peroxisome proliferator-activated receptor γ (PPARγ)-retinoid X receptor α (RXRα) heterodimer. This structure provided the first indication of direct interactions between the DNA-binding domain (DBD) and ligand-binding domain (LBD). In this study, we investigated whether there is a similar interface between the DNA- and ligand-binding domains for the androgen receptor (AR). Despite the structural differences between the AR- and PPARγ-LBD, a combination of in silico modeling and docking pointed out a putative interface between AR-DBD and AR-LBD. The surfaces were subjected to a point mutation analysis, which was inspired by known AR mutations described in androgen insensitivity syndromes and prostate cancer. Surprisingly, AR-LBD mutations D695N, R710A, F754S, and P766A induced a decrease in DNA binding but left ligand binding unaffected, while the DBD-residing mutations K590A, K592A, and E621A lowered the ligand-binding but not the DNA-binding affinity. We therefore propose that these residues are involved in allosteric communications between the AR-DBD and AR-LBD.
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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.