7F6H

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

7F6H の概要

• エントリーDOI: 10.2210/pdb7f6h/pdb
• EMDBエントリー: 31480
• 分子名称: Bradykinin receptor BK2R, Bradykinin, Guanine nucleotide-binding protein G(q) subunit alpha, ... (6 entities in total)
• 機能のキーワード: gpcr, bradykinin receptor, membrane protein
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 180163.97

構造登録者

Shen, J.,Zhang, D.,Fu, Y.,Chen, A.,Zhang, H. (登録日: 2021-06-25, 公開日: 2022-01-05, 最終更新日: 2024-10-23)

主引用文献

Shen, J.,Zhang, D.,Fu, Y.,Chen, A.,Yang, X.,Zhang, H.
Cryo-EM structures of human bradykinin receptor-G q proteins complexes.
Nat Commun, 13:714-714, 2022

PubMed 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-G 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 W283, 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 G proteins. Our structures elucidate the molecular mechanisms for the ligand binding, receptor activation, and G proteins coupling of B2R.

PubMed: 35132089
DOI: 10.1038/s41467-022-28399-1

実験手法

ELECTRON MICROSCOPY (2.9 Å)