CRCU

Chemical Research in Chinese Universities ›› 2012, Vol. 28 ›› Issue (3): 493-499.

• Articles • Previous Articles     Next Articles

Activation of β2-Adrenergic Receptor Induced by Three Catecholamine Agonists: a Docking and Molecular Dynamics Study

ZHANG Rui1,2, DONG Li-hua2, LING Bao-ping3, WANG Zhi-guo2, LIU Yong-jun2,3   

  1. 1. Shandong Key Laboratory of Edible Mushroom Technology, School of Life Sciences, Ludong University, Yantai 264025, P. R. China;
    2. Key Laboratory of Adaptation and Evolution of Plateau Biota, Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, P. R. China;
    3. School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, P. R. China
  • Received:2011-09-19 Revised:2012-02-04 Online:2012-05-25 Published:2012-05-03
  • Contact: LIU Yong-jun E-mail:yongjunliu_1@sdu.edu.cn
  • Supported by:

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

PDF (PC)

Abstract: We studied the activation of β2-adrenergic receptor(β2AR) by norepinephrine, epinephrine and isoproterenol 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 activators. We also simulated the change of the conformation of β2AR in the transmembrane regions(TMs), in the molecular switches, and in the conserved DRY(Aspartic acid, Arginine and Tyrosine) motif. This study provides detailed information concerning the structure of β2AR during activation process.

Key words: β2-Adrenergic receptor(β2AR), G Protein coupled receptor(GPCR), Molecular dynamics, Agonist, Activation