View source for 7vni


==AHR-ARNT PAS-B heterodimer==
<StructureSection load='7vni' size='340' side='right'caption='[[7vni]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vni]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VNI 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]] 1.997&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7vni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vni OCA], [https://pdbe.org/7vni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vni RCSB], [https://www.ebi.ac.uk/pdbsum/7vni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vni 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 7vni" style="background-color:#fffaf0;"></div>

==See Also==
*[[3D structures of hypoxia-inducible factor|3D structures of hypoxia-inducible factor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Dai SY]]