7BB6
AVP-V2R-Galphas-beta1-gamma2-Nb35 (L state)
Summary for 7BB6
| Entry DOI | 10.2210/pdb7bb6/pdb |
| EMDB information | 12128 |
| Descriptor | Vasopressin V2 receptor, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, ... (6 entities in total) |
| Functional Keywords | signaling protein, g protein-coupled receptor, hormone, vasopressin, v2r, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 158206.95 |
| Authors | Bous, J.,Mouillac, B.,Bron, P.,Granier, S.,Floquet, N.,Leyrat, C. (deposition date: 2020-12-17, release date: 2021-06-02, Last modification date: 2024-10-23) |
| Primary citation | Bous, J.,Orcel, H.,Floquet, N.,Leyrat, C.,Lai-Kee-Him, J.,Gaibelet, G.,Ancelin, A.,Saint-Paul, J.,Trapani, S.,Louet, M.,Sounier, R.,Demene, H.,Granier, S.,Bron, P.,Mouillac, B. Cryo-electron microscopy structure of the antidiuretic hormone arginine-vasopressin V2 receptor signaling complex. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: The antidiuretic hormone arginine-vasopressin (AVP) forms a signaling complex with the V2 receptor (V2R) and the G protein, promoting kidney water reabsorption. Molecular mechanisms underlying activation of this critical G protein-coupled receptor (GPCR) signaling system are still unknown. To fill this gap of knowledge, we report here the cryo-electron microscopy structure of the AVP-V2R-G complex. Single-particle analysis revealed the presence of three different states. The two best maps were combined with computational and nuclear magnetic resonance spectroscopy constraints to reconstruct two structures of the ternary complex. These structures differ in AVP and G binding modes. They reveal an original receptor-G interface in which the Gα subunit penetrates deep into the active V2R. The structures help to explain how V2R R137H or R137L/C variants can lead to two severe genetic diseases. Our study provides important structural insights into the function of this clinically relevant GPCR signaling complex. PubMed: 34020960DOI: 10.1126/sciadv.abg5628 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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