Activation of β_2-Adrenergic Receptor Induced by Three Catecholamine Agonists:a Docking and Molecular Dynamics Study

作     者：ZHANG Rui DONG Li-hua LING Bao-ping WANG Zhi-guo LIU Yong-jun 

作者机构：Shandong Key Laboratory of Edible Mushroom TechnologySchool of Life SciencesLudong UniversityYantai 264025P.R.China Key Laboratory of Adaptation and Evolution of Plateau BiotaNorthwest Institute of Plateau BiologyChinese Academy of SciencesXining 810008P.R.China School of Chemistry and Chemical EngineeringShandong UniversityJinan 250100P.R.China 

出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究（英文版）)

年 卷 期：2012年第28卷第3期

页      面：493-499页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 070205[理学-凝聚态物理] 08[工学] 0817[工学-化学工程与技术] 080501[工学-材料物理与化学] 0805[工学-材料科学与工程（可授工学、理学学位）] 0702[理学-物理学] 

基　　金：Supported by the Young and Middle-Aged Scientists Research Awards Foundation of Shangdong Province,China(No.BS2011SW002) the Research Foundation for Advanced Talents of Ludong University,China(No.LY2011017) 

主　　题：β2-Adrenergic receptor(β2AR) G Protein coupled receptor(GPCR) Molecular dynamics Agonist Activa-tion 

摘      要：We studied the activation of β2-adrenergic receptor（β2AR） by norepinephrine, epinephrine and isoprote- renol using docking and molecular dynamics（MD） simulation. The simulation was done on the assumption that β2AR was surrounded with explicit water and infinite lipid bilayer membrane at body temperature. So the result should be close to that under the physiological conditions. We calculated the structure of binding sites in β2AR for the three ac- tivators. We also simulated the change of the conformation ofβ2AR in the transmembrane regions（TMs）, in the mo- lecular switches, and in the conserved DRY（Aspartic acid, Arginine and Tyrosine） motif. This study provides detailed information concerning the structure ofβ2AR during activation process.