8ieb
From Proteopedia
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<table><tr><td colspan='2'>[[8ieb]] is a 2 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=8IEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IEB FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ieb]] is a 2 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=8IEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IEB 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]] 3.03Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.03Å</td></tr> | ||
| - | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand= | + | <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=8ieb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ieb OCA], [https://pdbe.org/8ieb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ieb RCSB], [https://www.ebi.ac.uk/pdbsum/8ieb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ieb ProSAT]</span></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=8ieb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ieb OCA], [https://pdbe.org/8ieb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ieb RCSB], [https://www.ebi.ac.uk/pdbsum/8ieb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ieb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/GP156_HUMAN GP156_HUMAN] The disease is caused by variants affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/GP156_HUMAN GP156_HUMAN] Orphan receptor. | + | [https://www.uniprot.org/uniprot/GP156_HUMAN GP156_HUMAN] Orphan G-protein coupled receptor involved in the regulation of hair cell orientation in mechanosensory organs of the inner ear. It is required to trigger a 180 degree reversal in hair cell orientation, creating a virtual line of polarity reversal (LPR) across which stereociliary bundles are arranged in opposite orientations.[UniProtKB:Q6PCP7] |
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8ieb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Cryo-EM structure of GPR156 of GPR156-miniGo-scFv16 complex (local refine)
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Categories: Homo sapiens | Large Structures | Cho Y | Park J | Shin J
