Structural Insights into the Activation of Human Aryl Hydrocarbon Receptor by the Environmental Contaminant Benzo[a]pyrene and Structurally Related Compounds
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The aryl hydrocarbon receptor (AHR) is a ligand-dependent transcription factor belonging to the bHLH/PAS protein family and responding to hundreds of natural and chemical substances. It is primarily involved in the defense against chemical insults and bacterial infections or in the adaptive immune response, but also in the development of pathological conditions ranging from inflammatory to neoplastic disorders. Despite its prominent roles in many (patho)physiological processes, the lack of high-resolution structural data has precluded for thirty years an in-depth understanding of the structural mechanisms underlying ligand-binding specificity, promiscuity and activation of AHR. We recently reported a cryogenic electron microscopy (cryo-EM) structure of human AHR bound to the natural ligand indirubin, the chaperone Hsp90 and the co-chaperone XAP2 that provided the first experimental visualization of its ligand-binding PAS-B domain. Here, we report a 2.75 Å resolution structure of the AHR complex bound to the environmental pollutant benzo[a]pyrene (B[a]P). The structure substantiates the existence of a bipartite PAS-B ligand-binding pocket with a geometrically constrained primary binding site controlling ligand binding specificity and affinity, and a secondary binding site contributing to the binding promiscuity of AHR. We also report a docking study of B[a]P congeners that validates the B[a]P-bound PAS-B structure as a suitable model for accurate computational ligand binding assessment. Finally, comparison of our agonist-bound complex with the recently reported structures of mouse and fruit fly AHR PAS-B in different activation states suggests a ligand-induced loop conformational change potentially involved in the regulation of AHR function.
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Compared to two recently published structures of AHR cytosolic complexes bound to Indirubin and BaP, these two ligands demonstrate similar binding patterns within the AHR-ARNT complexes.
“Notably, compared to two recently published structures of AHR cytosolic complexes bound to Indirubin and BaP29,40, these two ligands demonstrate similar binding patterns within the AHR-ARNT complexes (Supplementary Fig. 7g, h)”
From Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex (2025) · cites this paper as [40]
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“Notably, compared to two recently published structures of AHR cytosolic complexes bound to Indirubin and BaP 29,40 , these two ligands demonstrate similar binding patterns within the AHR-ARNT complexes (Supplementary Fig.”
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Structural context matters when interpreting clozapine AHR docking
Wu, L., & Wei, X. (2026) · Archives of Toxicology · doi:10.1007/s00204-026-04590-x
- Authors
- Kwong, H.-S., Paloni, M., Grandvuillemin, L., Sirounian, S., Ancelin, A., Lai-Kee-Him, J., Grimaldi, M., Carivenc, C., Lancey, C., Ragan, T. J., Hesketh, E. L., Balaguer, P., Barducci, A., Gruszczyk, J., & Bourguet, W.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Inserm (FR)
- University of Leicester (GB)
- Corresponding author
- Gruszczyk, Jakub
- Bourguet, William
- ORCID
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2024-02
- Volume
- 436
- Issue
- 3
- Pages
- 168411
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W4389990488
- Cited by
- 40
- References
- 52
- Citations by year
- 2026: 19 · 2025: 15 · 2024: 6
- FWCI
- 4.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Molecular Biology (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by-sa)
- Funders
- Agence Nationale de la Recherche (ANR-16-IDEX-0006, ANR-21-EXES-0005)
- Pakistan Agricultural Research Council
- European Commission (101057014, 825489)
- Medical Research Council (MC_PC_17136)
- Topics
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Toxic Organic Pollutants Impact
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- aryl hydrocarbon receptor, benzo[a]pyrene, PAS-B domain, ligand specificity, receptor activation, environmental pollutants, ligand-induced conformational change, cryo-EM structure, molecular docking, HSP90, bHLH-PAS transcription factors
- MeSH terms
- Protein Domains, Benzo(a)pyrene, Binding Sites, Environmental Pollutants, Humans, Ligands, Receptors, Aryl Hydrocarbon
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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