7R0C

Structure of the AVP-V2R-arrestin2-ScFv30 complex

Summary for 7R0C

• Entry DOI: 10.2210/pdb7r0c/pdb
• EMDB information: 14221
• Descriptor: Vasopressin V2 receptor, AVP, Arrestin2, ... (4 entities in total)
• Functional Keywords: g-protein coupled receptor v2 receptor arrestin 2 vasopressin, membrane protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 119853.25

Authors

Bous, J.,Fouillen, A.,Trapani, S.,Granier, S.,Mouillac, B.,Bron, P. (deposition date: 2022-02-01, release date: 2022-09-14, Last modification date: 2024-10-23)

Primary citation

Bous, J.,Fouillen, A.,Orcel, H.,Trapani, S.,Cong, X.,Fontanel, S.,Saint-Paul, J.,Lai-Kee-Him, J.,Urbach, S.,Sibille, N.,Sounier, R.,Granier, S.,Mouillac, B.,Bron, P.
Structure of the vasopressin hormone-V2 receptor-beta-arrestin1 ternary complex.
Sci Adv, 8:eabo7761-eabo7761, 2022

PubMed Abstract: Arrestins interact with G protein-coupled receptors (GPCRs) to stop G protein activation and to initiate key signaling pathways. Recent structural studies shed light on the molecular mechanisms involved in GPCR-arrestin coupling, but whether this process is conserved among GPCRs is poorly understood. Here, we report the cryo-electron microscopy active structure of the wild-type arginine-vasopressin V2 receptor (V2R) in complex with β-arrestin1. It reveals an atypical position of β-arrestin1 compared to previously described GPCR-arrestin assemblies, associated with an original V2R/β-arrestin1 interface involving all receptor intracellular loops. Phosphorylated sites of the V2R carboxyl terminus are clearly identified and interact extensively with the β-arrestin1 N-lobe, in agreement with structural data obtained with chimeric or synthetic systems. Overall, these findings highlight a notable structural variability among GPCR-arrestin signaling complexes.

PubMed: 36054364
DOI: 10.1126/sciadv.abo7761

Experimental method

ELECTRON MICROSCOPY (4.73 Å)