7F24

Cryo-EM structure of the GTP-bound dopamine receptor 1 and mini-Gs complex without Nb35

7F24 の概要

• エントリーDOI: 10.2210/pdb7f24/pdb
• EMDBエントリー: 31427
• 分子名称: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,Isoform Gnas-2 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, D(1A) dopamine receptor, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (6 entities in total)
• 機能のキーワード: gpcr, dopamine receptor, mini-gs, membrane protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 129256.86

構造登録者

Xiao, T.,Zheng, S. (登録日: 2021-06-10, 公開日: 2022-06-15, 最終更新日: 2025-07-02)

主引用文献

Teng, X.,Chen, S.,Wang, Q.,Chen, Z.,Wang, X.,Huang, N.,Zheng, S.
Structural insights into G protein activation by D1 dopamine receptor.
Sci Adv, 8:eabo4158-eabo4158, 2022

PubMed Abstract: G protein-coupled receptors (GPCRs) comprise the largest family of membrane receptors and are the most important drug targets. An agonist-bound GPCR engages heterotrimeric G proteins and triggers the exchange of guanosine diphosphate (GDP) with guanosine triphosphate (GTP) to promote G protein activation. A complete understanding of molecular mechanisms of G protein activation has been hindered by a lack of structural information of GPCR-G protein complex in nucleotide-bound states. Here, we report the cryo-EM structures of the D1 dopamine receptor and mini-G complex in the nucleotide-free and nucleotide-bound states. These structures reveal major conformational changes in Gα such as structural rearrangements of the carboxyl- and amino-terminal α helices that account for the release of GDP and the GTP-dependent dissociation of Gα from Gβγ subunits. As validated by biochemical and cellular signaling studies, our structures shed light into the molecular basis of the entire signaling events of GPCR-mediated G protein activation.

PubMed: 35687690
DOI: 10.1126/sciadv.abo4158

実験手法

ELECTRON MICROSCOPY (4.16 Å)