5G53

Structure of the adenosine A2A receptor bound to an engineered G protein

5G53 の概要

• エントリーDOI: 10.2210/pdb5g53/pdb
• 分子名称: ADENOSINE RECEPTOR A2A, ENGINEERED DOMAIN OF HUMAN G ALPHA S LONG ISOFORM, N-ETHYL-5'-CARBOXAMIDO ADENOSINE, ... (5 entities in total)
• 機能のキーワード: signaling protein, g protein coupled receptor, adenosine receptor, seven-helix receptor, integral membrane protein, gpcr, engineered g protein, gpcr-g protein complex, mini-gs
• 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: 124745.90

構造登録者

Carpenter, B.,Nehme, R.,Warne, T.,Leslie, A.G.W.,Tate, C.G. (登録日: 2016-05-19, 公開日: 2016-08-03, 最終更新日: 2024-11-13)

主引用文献

Carpenter, B.,Nehme, R.,Warne, T.,Leslie, A.G.W.,Tate, C.G.
Structure of the Adenosine A2A Receptor Bound to an Engineered G Protein
Nature, 536:104-, 2016

PubMed Abstract: G-protein-coupled receptors (GPCRs) are essential components of the signalling network throughout the body. To understand the molecular mechanism of G-protein-mediated signalling, solved structures of receptors in inactive conformations and in the active conformation coupled to a G protein are necessary. Here we present the structure of the adenosine A(2A) receptor (A(2A)R) bound to an engineered G protein, mini-Gs, at 3.4 Å resolution. Mini-Gs binds to A(2A)R through an extensive interface (1,048 Å2) that is similar, but not identical, to the interface between Gs and the β2-adrenergic receptor. The transition of the receptor from an agonist-bound active-intermediate state to an active G-protein-bound state is characterized by a 14 Å shift of the cytoplasmic end of transmembrane helix 6 (H6) away from the receptor core, slight changes in the positions of the cytoplasmic ends of H5 and H7 and rotamer changes of the amino acid side chains Arg3.50, Tyr5.58 and Tyr7.53. There are no substantial differences in the extracellular half of the receptor around the ligand binding pocket. The A(2A)R-mini-Gs structure highlights both the diversity and similarity in G-protein coupling to GPCRs and hints at the potential complexity of the molecular basis for G-protein specificity.

PubMed: 27462812
DOI: 10.1038/NATURE18966

実験手法

X-RAY DIFFRACTION (3.4 Å)