8IEB
Cryo-EM structure of GPR156 of GPR156-miniGo-scFv16 complex (local refine)
This is a non-PDB format compatible entry.
Summary for 8IEB
| Entry DOI | 10.2210/pdb8ieb/pdb |
| EMDB information | 35377 |
| Descriptor | Probable G-protein coupled receptor 156, [(2R)-3-[(E)-hexadec-9-enoyl]oxy-2-octadecanoyloxy-propyl] 2-(trimethylazaniumyl)ethyl phosphate (2 entities in total) |
| Functional Keywords | membrane protein, g-protein coupled receptor, signal transduction, phospholipid, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 132777.12 |
| Authors | |
| Primary citation | Shin, J.,Park, J.,Jeong, J.,Lam, J.H.,Qiu, X.,Wu, D.,Kim, K.,Lee, J.Y.,Robinson, C.V.,Hyun, J.,Katritch, V.,Kim, K.P.,Cho, Y. Constitutive activation mechanism of a class C GPCR. Nat.Struct.Mol.Biol., 31:678-687, 2024 Cited by PubMed Abstract: 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 signaling contributes to loss of hearing. Here we present the cryo-electron microscopy structures of human GPR156 in the G-free and G-coupled states. We found that an endogenous phospholipid molecule is located within each TMD of the GPR156 dimer. Asymmetric binding of Gα 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. PubMed: 38332368DOI: 10.1038/s41594-024-01224-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.03 Å) |
Structure validation
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