View source for 7vnh


==drosophlia AHR PAS-B domain bound by the antagonist alpha-naphthoflavone==
<StructureSection load='7vnh' size='340' side='right'caption='[[7vnh]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vnh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VNH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.402&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BHF:2-PHENYL-4H-BENZO[H]CHROMEN-4-ONE'>BHF</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7vnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vnh OCA], [https://pdbe.org/7vnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vnh RCSB], [https://www.ebi.ac.uk/pdbsum/7vnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vnh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E1JIM6_DROME E1JIM6_DROME] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:36266304</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vnh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Dai SY]]