EMD-31480

Single-particle
2.9 Å
EMD-31480 Deposition: 25/06/2021
Map released: 05/01/2022
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-31480

Cryo-EM structure of human bradykinin receptor BK2R in complex Gq proteins and bradykinin

EMD-31480

Single-particle
2.9 Å
EMD-31480 Deposition: 25/06/2021
Map released: 05/01/2022
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: Bradykinin receptor BK2RR in complex with Gq proteins and bradykinin
Fitted models: 7f6h (Avg. Q-score: 0.554)

Deposition Authors: Shen J , Zhang D
Cryo-EM structures of human bradykinin receptor-G q proteins complexes.
Shen J , Zhang D , Fu Y , Chen A , Yang X , Zhang H
(2022) Nat Commun , 13 , 714 - 714
PUBMED: 35132089
DOI: doi:10.1038/s41467-022-28399-1
ISSN: 2041-1723
Abstract:
The type 2 bradykinin receptor (B2R) is a G protein-coupled receptor (GPCR) in the cardiovascular system, and the dysfunction of B2R leads to inflammation, hereditary angioedema, and pain. Bradykinin and kallidin are both endogenous peptide agonists of B2R, acting as vasodilators to protect the cardiovascular system. Here we determine two cryo-electron microscopy (cryo-EM) structures of human B2R-Gq in complex with bradykinin and kallidin at 3.0 Å and 2.9 Å resolution, respectively. The ligand-binding pocket accommodates S-shaped peptides, with aspartic acids and glutamates as an anion trap. The phenylalanines at the tail of the peptides induce significant conformational changes in the toggle switch W2836.48, the conserved PIF, DRY, and NPxxY motifs, for the B2R activation. This further induces the extensive interactions of the intracellular loops ICL2/3 and helix 8 with Gq proteins. Our structures elucidate the molecular mechanisms for the ligand binding, receptor activation, and Gq proteins coupling of B2R.