8iec

Cryo-EM structure of miniGo-scFv16 of GPR156-miniGo-scFv16 complex (local refine)

spinqualitylabelsall models 8iec, resolution 3.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8iec is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.18Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease GNAO_HUMAN Early infantile epileptic encephalopathy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function GNAO_HUMAN Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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