View source for 8ieq


==Cryo-EM structure of G-protein free GPR156==
<StructureSection load='8ieq' size='340' side='right'caption='[[8ieq]], [[Resolution|resolution]] 2.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ieq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IEQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.73&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1LYA:[(2~{R})-3-[(~{E})-hexadec-9-enoyl]oxy-2-octadecanoyloxy-propyl]+2-(trimethylazaniumyl)ethyl+phosphate'>A1LYA</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=8ieq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ieq OCA], [https://pdbe.org/8ieq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ieq RCSB], [https://www.ebi.ac.uk/pdbsum/8ieq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ieq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Class C G-protein-coupled receptors (GPCRs) are activated through binding of agonists to the large extracellular domain (ECD) followed by rearrangement of the transmembrane domains (TMDs). GPR156, a class C orphan GPCR, is unique because it lacks an ECD and exhibits constitutive activity. Impaired GPR156-G(i) signaling contributes to loss of hearing. Here we present the cryo-electron microscopy structures of human GPR156 in the G(o)-free and G(o)-coupled states. We found that an endogenous phospholipid molecule is located within each TMD of the GPR156 dimer. Asymmetric binding of Galpha to the phospholipid-bound GPR156 dimer restructures the first and second intracellular loops and the carboxy-terminal part of the elongated transmembrane 7 (TM7) without altering dimer conformation. Our findings reveal that GPR156 is a transducer for phospholipid signaling. Constant binding of abundant phospholipid molecules and the G-protein-induced reshaping of the cytoplasmic face provide a basis for the constitutive activation of GPR156.

Constitutive activation mechanism of a class C GPCR.,Shin J, Park J, Jeong J, Lam JH, Qiu X, Wu D, Kim K, Lee JY, Robinson CV, Hyun J, Katritch V, Kim KP, Cho Y Nat Struct Mol Biol. 2024 Apr;31(4):678-687. doi: 10.1038/s41594-024-01224-7. , Epub 2024 Feb 8. PMID:38332368<ref>PMID:38332368</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ieq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cho Y]]
[[Category: Park J]]
[[Category: Shin J]]