7EWL
cryo-EM structure of apo GPR158
Summary for 7EWL
| Entry DOI | 10.2210/pdb7ewl/pdb |
| Related | 7EWP 7EWR |
| EMDB information | 31351 |
| Descriptor | Probable G-protein coupled receptor 158 (1 entity in total) |
| Functional Keywords | class c orphan gpcr, depression, neuronal signaling, pas-folded gpcr, noncanonical signaling gpcr, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 154925.41 |
| Authors | |
| Primary citation | Jeong, E.,Kim, Y.,Jeong, J.,Cho, Y. Structure of the class C orphan GPCR GPR158 in complex with RGS7-G beta 5. Nat Commun, 12:6805-6805, 2021 Cited by PubMed Abstract: GPR158, a class C orphan GPCR, functions in cognition, stress-induced mood control, and synaptic development. Among class C GPCRs, GPR158 is unique as it lacks a Venus flytrap-fold ligand-binding domain and terminates Gαi/o protein signaling through the RGS7-Gβ5 heterodimer. Here, we report the cryo-EM structures of GPR158 alone and in complex with one or two RGS7-Gβ5 heterodimers. GPR158 dimerizes through Per-Arnt-Sim-fold extracellular and transmembrane (TM) domains connected by an epidermal growth factor-like linker. The TM domain (TMD) reflects both inactive and active states of other class C GPCRs: a compact intracellular TMD, conformations of the two intracellular loops (ICLs) and the TMD interface formed by TM4/5. The ICL2, ICL3, TM3, and first helix of the cytoplasmic coiled-coil provide a platform for the DHEX domain of one RGS7 and the second helix recruits another RGS7. The unique features of the RGS7-binding site underlie the selectivity of GPR158 for RGS7. PubMed: 34815401DOI: 10.1038/s41467-021-27147-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.52 Å) |
Structure validation
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