Beili Wu is currently a Principal Investigator at Shanghai Institute of Materia Medica (SIMM), Chinese Academy of Sciences (CAS). She got her B.S. degree from Beijing Normal University in 2001 and her Ph. D. degree in biophysics from Tsinghua University, Beijing in 2006. She then worked as a postdoc fellow at The Scripps Research Institute in La Jolla, California from 2007 to 2011. She received the "Hundred Talent Plan" award from CAS and started her own research group at SIMM in 2011.
Dr. Wu’s current research is focused on a deep understanding of the structural basis of G protein-coupled receptor (GPCR) signaling transduction, leading to the development of new therapeutics for severe human diseases. Her lab has solved high-resolution crystal structures of 6 GPCRs. These structures reveal binding modes between different receptors and their selective ligands, and provide insights into the molecular mechanisms of GPCR signal recognition and modulation. The findings deepen the understanding of GPCR signal transduction and will facilitate drug development for the treatment of HIV infection, thrombosis and diabetes. In the recent five years, Dr. Wu published eight papers in Science, Nature and Cell, and is the corresponding author in five of the papers. She has received many awards, including "Outstanding Young Female Scientist Award in China", "TanJiaZhen Life Science Innovation Award", "Outstanding Achievement Award in Life Chemistry" by WuXi AppTec and "ShuLan Young Scientist Award in Medical Science".
Structural studies and drug discovery of G protein-coupled receptors
G protein-coupled receptors (GPCRs), which comprise the largest membrane protein family in human genome, play critical roles in cell signal transduction. These receptors are involved in many human diseases, and represent the targets of over 40% of modern medicinal drugs. GPCR structures provide important foundations for functional studies, and are required for drug discovery. However, structure determination of GPCRs remains extremely challenging. Dr. Wu’s group determined the crystal structure of chemokine receptor CCR5 that acts as a co-receptor of the Human Immunodeficiency Virus (HIV). The CCR5 structure provides insights into the interaction between HIV and human cells and the anti-HIV mechanisms of different drugs, laying a foundation for carrying out next generation anti-HIV drug discovery. Her team also solved the structures of two important anti-thrombotic drug targets, purinergic receptors P2Y1R and P2Y12R, which, for the first time, reveal a novel ligand binding site on the external receptor surface and the interactions between these two receptors and different drugs. These structural findings should enable discovery of new antithrombotic drugs. Recently, Dr. Wu and her team successfully determined the first crystal structure of a full-length class B GPCR, which sheds light on the cooperative modulation mechanism of different domains on receptor activation, greatly deepening the understanding of the relationship between the structure and function of GPCRs. These high-resolution insights into GPCRs advance the studies of the molecular mechanisms of GPCR signal recognition, transduction and modulation, and provide important structural basis for drug development of severe diseases.