时间：11月16日星期二10:00-11:30    

Time：10:00-11:30 AM，Tues., Nov. 16，2021

地点：西湖大学云栖校区3号楼312会议室

Venue: Room 312, 3F, Building 3, Yunqi Campus

主持人：西湖大学生命科学学院研究员 卢培龙

Host：Dr. Peilong Lu, School of Life Sciences

主讲嘉宾/Speaker:

Dr. Huaqiang Eric Xu, Shanghai Institute of Materia Medica, Chinese Academy of Sciences

Dr. H. Eric Xu is a world renowned structural biologist and the founding Director of the CAS Key Laboratory of Receptor Research at Shanghai Institute of Materia Medica, Chinese Academy of Sciences. He has published more than 220 papers which have been cited over 26,000 times, including fourteen in Nature and eight in Science. Two papers on plant hormone signaling were selected as one of the top ten breakthroughs by Science (2009) and by Chinese Academy of Sciences (2014). His X-ray laser structure of the first GPCR-arrestin complex was also selected as a top 10 breakthrough by Chinese Academy of Sciences in 2015 and was recognized by the 2016 Hans Neurath Award of Protein Society and the 2016 Wuxi outstanding achievement award. He also has been awarded the Shanghai "Magnolia Memorial Award" and the 13th "C.C. Tan Life Science Achievement Award" in 2020 and 2021, respectively.

讲座摘要/Abstract:

Cell-cell communication and their functional coordination are a fundamental process of living organisms. Hormones, including small molecule neurotransmitters, peptides, and secreted proteins, are the most effective mediators of cell-to-cell signaling transduction.   Hormone recognition by their receptors is the first step of hormone-mediated signal transduction. Two major classes of hormone receptors are nuclear receptors and G protein coupled receptors (GPCRs), which are also two major classes of drug targets. For the past two decades, our laboratory has been focusing on the structure and function of hormone receptors as well as structured based drug discovery. In this talk, I will first present our works on nuclear receptors by revealing the overall helical sandwiched fold of the their ligand-binding domains (LBD) and the topology of ligand binding pocket. Using the glucocorticoid receptor (GR) as an example, I will display how the ligand binding pocket will changes its topology to accommodate its bound ligands, and how this information was used to design a new generation of glucocorticoid drug with reduced side effects. I will then move on to our works in the area of GPCRs, which functions are mediated primarily through two pathways, G protein and arrestin. Biased ligands that selectively activated either G protein or arrestin pathways often display better safety profile than the balanced ligand that activated both pathways, thus biased ligands have become a new paradigm of GPCR drug discovery. Over the past 15 years, our laboratory have solved the structures of the first GPCR-arrestin complex as well as the first set of structures of GPCR in complex with the inhibitory G protein Gi. In the past two years, our lab have solved over 100 structures of GPCR-G protein complexes, which should pave the road for future drug discovery on this important class of drug targets.

联系人/Contact：

生命科学学院

于文越 yuwenyue@westlake.edu.cn