We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

7vnh

From Proteopedia

Jump to: navigation, search

drosophlia AHR PAS-B domain bound by the antagonist alpha-naphthoflavone

Structural highlights

7vnh is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.402Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

E1JIM6_DROME

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.

References

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