A model for recognition of polychlorinated dibenzo‐p‐dioxins by the aryl hydrocarbon receptor
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Ligand binding by the aryl hydrocarbon receptor (AhR), a member of the bHLH‐PAS family of transcriptional regulatory proteins, has been mapped to a region within the second ‘PAS’ domain, a conserved sequence motif first discovered in the Per‐ARNT‐Sim family of proteins. In addition to the bacterial photoactive yellow protein (PYP), which had been proposed as a structural prototype for the three dimensional fold of PAS domains, two crystal structures of the PAS domain have recently been determined: the human potassium channel HERG and the heme binding domain of the bacterial O 2 sensing FixL protein. The three structures reveal a highly conserved structural framework in evolutionary rather distant PAS domains, provide a more general view of how these domains can recognize their ligands and suggest a structure–function relationship that we exploited to build a three‐dimensional model of the ligand binding domain (LBD) of the mouse aryl hydrocarbon receptor (mAhR). The model allowed us to putatively identify the residues responsible for the recognition of polychlorinated dibenzo‐p‐dioxins (PCDDs) by AhR receptors and to formulate an hypothesis on the signal transduction mechanism.
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The first models derived for the mAhR LBD, based on FixL and Phy3 as templates, were not optimal due to the low degree of sequence similarity with the templates and the consequential uncertainty in the alignment of some regions.
“It is likely that the first models we derived for the mAhR LBD, based on the only available PAS structures at that time [with FixL (23) and Phy3 (26) as templates], were not optimal due to the low degree of sequence similarity with the templates and the consequential uncertainty in the alignment of some regions.”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [23]
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- Authors
- Procopio, M., Lahm, A., Tramontano, A., Bonati, L., & Pitea, D.
- Affiliations
- University of Milano-Bicocca (IT)
- Institute of Molecular Biology and Pathology (IT)
- Sapienza University of Rome (IT)
- Corresponding author
- Tramontano, A.
- ORCID
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 2002-01
- Volume
- 269
- Issue
- 1
- Pages
- 13-18
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1511999067
- Cited by
- 61
- References
- 27
- Citations by year
- 2025: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2017: 3 · 2016: 1 · 2015: 1 · 2013: 2 · 2012: 2
- FWCI
- 2.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- aryl hydrocarbon receptor, polychlorinated dibenzo-p-dioxins, ligand-binding domain, PAS domain, bHLH-PAS transcription factors, structure-function relationship, 3D model, ligand recognition, signal transduction, hERG
- MeSH terms
- Polychlorinated Dibenzodioxins, Amino Acid Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Receptors, Aryl Hydrocarbon
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