Ligand Promiscuity of Aryl Hydrocarbon Receptor Agonists and Antagonists Revealed by Site-Directed Mutagenesis
Open accessAbstract
The aryl hydrocarbon receptor (AhR) is a ligand-dependent transcription factor that can be activated by structurally diverse chemicals. To examine the mechanisms responsible for the promiscuity in AhR ligand binding, we determined the effects of mutations within the AhR ligand-binding domain (LBD) on the activity of diverse AhR ligands. Site-directed mutagenesis identified Ile319 of the mouse AhR and, to a lesser extent, Phe318 as residues involved in ligand-selective modulation of AhR transformation using a panel of 12 AhR ligands. These ligands could be categorized into four distinct structurally related groups based on their ability to activate AhR mutants at position 319 in vitro. The mutation I319K was selectively activated by FICZ and not by other examined ligands in vitro and in cell culture. F318L and F318A mutations resulted in the conversion of AhR agonists β-naphthoflavone and 3-methylcholanthrene, respectively, into partial agonists/antagonists. Hsp90 binding to the AhR was decreased with several mutations and was inversely correlated with AhR ligand-binding promiscuity. Together, these data define overlapping amino acid residues within the AhR LBD involved in the selectivity of ligand binding, the agonist or antagonist mode of ligand binding, and hsp90 binding and provide insights into the ligand diversity of AhR activators.
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Studies revealed significant differences in interactions between structurally diverse ligands and residues within the AhR ligand binding domain, accounting for the observed promiscuity.
“These studies revealed significant differences in the interactions between structurally diverse ligands and residues within the AhR ligand binding domain (LBD), that account for the observed promiscuity18.”
From Modeling the binding of diverse ligands within the Ah receptor ligand binding domain (2019) · cites this paper as [18]
The Abstract and the section “Mutations of Ile319 reveal a diversity of ligand-selective mechanisms” report that changing LBD residues produces different responses to structurally diverse ligands, supporting ligand-specific interactions. But the paper presents those interactions as a possible explanation for AhR promiscuity, rather than establishing that they account for it. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThe H320A mutation in mouse AHR (corresponding to H324A in porcine and H326A in human AHR) can reduce DNA-binding activity triggered by various agonists.
“Previous studies reported that the H320A mutation in mouse AHR (mAHR), located outside the PAS-B pocket (corresponding to H324A in porcine and H326A in human AHR), could reduce DNA-binding activity triggered by various agonists39.”
From Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex (2025) · cites this paper as [39]
The Results (Fig. 2B–C; page unavailable) test mouse H320A for ligand-dependent DNA binding and report that it was activated by every compound in the panel except ANF. The cited paper does not give the claimed porcine H324A or human H326A correspondences, and the retrieved text does not establish that H320 lies outside the PAS-B pocket. (LLM, conf=0.78)
Experimental — accuracy not yet measuredThe ten selected compounds are known AhR agonists.
“All these compounds are known to be AhR agonists18.”
From Modeling the binding of diverse ligands within the Ah receptor ligand binding domain (2019) · cites this paper as [18]
Similar ligand binding-decreasing effects were reported by other groups following point mutations of these key pocket residues.
“Similar ligand binding-decreasing effects were reported by other groups following point mutations of these key pocket residues39,43,44.”
From Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex (2025) · cites this paper as [39]
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- Authors
- Soshilov, A. A., & Denison, M. S.
- Affiliations
- University of California, Davis (US)
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2014-05-01
- Volume
- 34
- Issue
- 9
- Pages
- 1707-1719
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC3993610
- OpenAlex
- W1967885926
- Cited by
- 128
- References
- 66
- Citations by year
- 2026: 7 · 2025: 3 · 2024: 7 · 2023: 4 · 2022: 8 · 2021: 16 · 2020: 15 · 2019: 15 · 2018: 17 · 2017: 15 · 2016: 10 · 2015: 8 · 2014: 2
- FWCI
- 7.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Università degli Studi di Milano-Bicocca
- Division of Agriculture and Natural Resources, University of California
- National Institute of Environmental Health Sciences (R01-ES07685, P42ES004699, R01ES007685)
- Topics
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Toxic Organic Pollutants Impact
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Keywords
- aryl hydrocarbon receptor, ligand-binding domain, FICZ, beta-naphthoflavone, 3-methylcholanthrene, site-directed mutagenesis, transcription factor activation
- MeSH terms
- Animals, Binding Sites, Cell Line, Ligands, Models, Molecular, Protein Binding, Mutagenesis, Site-Directed, Receptors, Aryl Hydrocarbon, HSP90 Heat-Shock Proteins, Mice, Basic Helix-Loop-Helix Proteins
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