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Publication Abstract from PubMed

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.

Structural insight into the ligand binding mechanism of aryl hydrocarbon receptor.,Dai S, Qu L, Li J, Zhang Y, Jiang L, Wei H, Guo M, Chen X, Chen Y Nat Commun. 2022 Oct 20;13(1):6234. doi: 10.1038/s41467-022-33858-w. PMID:36266304^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.