Structural insight into the ligand binding mechanism of aryl hydrocarbon receptor

Shuyan Dai, Lingzhi Qu, Jun Li, Ye Zhang, Longying Jiang, Hudie Wei, Ming Guo, Xiaojuan Chen and Yongheng Chen ()
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Shuyan Dai: Central South University
Lingzhi Qu: Central South University
Jun Li: The First Affiliated Hospital of University of South China
Ye Zhang: Central South University
Longying Jiang: Central South University
Hudie Wei: Central South University
Ming Guo: Central South University
Xiaojuan Chen: Central South University
Yongheng Chen: Central South University

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract The aryl hydrocarbon receptor (AHR), a member of the basic helix–loop–helix (bHLH) Per–Arnt–Sim (PAS) family of transcription factors, plays important roles in regulating xenobiotic metabolism, cellular differentiation, stem cell maintenance, as well as immunity. More recently, AHR has gained significant interest as a drug target for the development of novel cancer immunotherapy drugs. Detailed understanding of AHR-ligand binding has been hampered for decades by the lack of a three-dimensional structure of the AHR PAS-B domain. Here, we present multiple crystal structures of the Drosophila AHR PAS-B domain, including its apo, ligand-bound, and AHR nuclear translocator (ARNT) PAS-B-bound forms. Together with biochemical and cellular assays, our data reveal structural features of the AHR PAS-B domain, provide insights into the mechanism of AHR ligand binding, and provide the structural basis for the future development of AHR-targeted therapeutics.

Date: 2022
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DOI: 10.1038/s41467-022-33858-w

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