+検索条件
-Structure paper
タイトル | Activation of the α adrenoceptor by the sedative sympatholytic dexmedetomidine. |
---|---|
ジャーナル・号・ページ | Nat Chem Biol, Vol. 16, Issue 5, Page 507-512, Year 2020 |
掲載日 | 2020年3月9日 |
著者 | Daopeng Yuan / Zhongmin Liu / Jonas Kaindl / Shoji Maeda / Jiawei Zhao / Xiaoou Sun / Jun Xu / Peter Gmeiner / Hong-Wei Wang / Brian K Kobilka / |
PubMed 要旨 | The α adrenergic receptors (αARs) are G protein-coupled receptors (GPCRs) that respond to adrenaline and noradrenaline and couple to the Gi/o family of G proteins. αARs play important roles in ...The α adrenergic receptors (αARs) are G protein-coupled receptors (GPCRs) that respond to adrenaline and noradrenaline and couple to the Gi/o family of G proteins. αARs play important roles in regulating the sympathetic nervous system. Dexmedetomidine is a highly selective αAR agonist used in post-operative patients as an anxiety-reducing, sedative medicine that decreases the requirement for opioids. As is typical for selective αAR agonists, dexmedetomidine consists of an imidazole ring and a substituted benzene moiety lacking polar groups, which is in contrast to βAR-selective agonists, which share an ethanolamine group and an aromatic system with polar, hydrogen-bonding substituents. To better understand the structural basis for the selectivity and efficacy of adrenergic agonists, we determined the structure of the αAR in complex with dexmedetomidine and Go at a resolution of 2.9 Å by single-particle cryo-EM. The structure reveals the mechanism of αAR-selective activation and provides insights into Gi/o coupling specificity. |
リンク | Nat Chem Biol / PubMed:32152538 |
手法 | EM (単粒子) |
解像度 | 2.9 - 4.1 Å |
構造データ | |
化合物 | ChemComp-CZX: |
由来 |
|
キーワード | MEMBRANE PROTEIN / GPCR / Complex / cryo-EM |