Xinquan WANG     Ph.D.


1990-1995, Fudan University, B. Sc.

1995-2000, Institute of Biophysics, Chinese Academy of Sciences, Ph.D.

2000-2003, Institute of Biophysics, Chinese Academy of Sciences, Research Associate.

2003-2008, Stanford University, Postdoctoral researcher

2008-present, Tsinghua University, Professor


Research interest

We use X-ray crystallography and other biochemical techniques to study how protein-protein interactions mediate the specific recognition of cytokines and growth factors by plasma membrane receptors, which is an important step in initiating cellular responses to the change of extracellular environment. Another growing interest in my group is structural and biochemical studies of protein complexes involved in virus-host interaction.

Selected publications

1.       Zuo T, Sun J, Wang G, Jiang L, Zuo Y, Li D, Shi X, Liu X, Fan S, Ren H, Hu H, Sun L, Zhou B, Liang M, Zhou P*, Wang X*, Zhang L*. Comprehensive analysis of antibody recognition in convalescent humans from highly pathogenic avian influenza H5N1 infection. Nature Communications 2015, 6:8855. doi: 10.1038/ncomms9855.

2.       Yu X, Zhang S, Jiang L, Cui Y, Li D, Wang D, Wang, N, Fu L, Shi X, Li Z, Zhang L*, Wang X*. Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27. Scientific Reports 2015, 5:13133. doi: 10.1038/srep13133.

3.       Wei H, Wang D, Qian Y, Liu X, Fan S, Yin H, Wang X*. Structural basis for the specific recognition of IL-18 by its alpha receptor. FEBS Letters 2014, 588 (21): 3838-3843.

4.       Jiang L, Wang N, Zuo T, Shi X, Poon KM, Wu Y, Gao F, Li D, Wang R, Guo J, Fu L, Yuen KY, Zheng BJ*, Wang X*, Zhang L*. Potent neutralization of MERS-CoV by human neutralizing monoclonal antibodies to the viral spike glycoprotein. Sci Transl Med. 2014, 6(234):234ra59. doi: 10.1126/scitranslmed.3008140.

5.       Mei K, Jin Z, Ren F, Wang Y, Chang Z*, Wang X*. Structural basis for the recognition of RNA polymerase II C-terminal domain by CREPT and p15RS. Sci China Life Sci 2014, 57: 97-106.

6.       Liu X, Hammel M, He Y, Tainer JA, Jeng US, Zhang L, Wang S*, Wang X*. Structural insights into the interaction of IL-33 with its receptors. Proc Natl Acad Sci USA. 2013, 110: 14918-23.

7.       Wang N, Shi X, Jiang L, Zhang S, Wang D, Tong P, Guo D, Fu L, Cui Y, Liu X, Arledge KC, Chen YH, Zhang L*, Wang X*. Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4. Cell Res. 2013, 23: 986-93.

8.       Wang D, Huang B, Zhang S, Yu X, Wu W, Wang X*. Structural basis for R-spondin recognition by LGR4/5/6 receptors. Genes Dev. 2013, 27: 1339-44.

9.       Liu X, Liu S, Feng Y, Liu J, Chen Y, Pham K, Deng H, Hirschi KD, Wang X*, Cheng NH*. (2013). Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts. Proc. Nat. Acad. Sci. USA 110, 9565-9560.

10.     Wang X*. Structural studies of GDNF family ligands with their receptors-Insights into ligand recognition and activation of receptor tyrosine kinase RET. Biochim Biophys Acta. 2013, 1834: 2205-12.

11.     Luan X, Lu Q, Jiang Y, Zhang S, Wang Q, Yuan H, Zhao W, Wang J, Wang X*. Crystal structure of human RANKL complexed with its decoy receptor osteoprotegerin. J Immunol. 2012, 189: 245-252.

12.     Li L, Wang D, Jiang Y, Sun J, Zhang S, Chen Y, Wang X*. Crystal structure of human ISG15 in complex with influenza B virus NS1B. J Biol. Chem. 2011, 286: 30258-30262.

13.     Xue X, Lu Q, Wei H, Wang D, Chen D, He G, Huang L, Wang H, Wang X*. Structural Basis of Chemokine Sequestration by CrmD, a Poxvirus-Encoded Tumor Necrosis Factor Receptor. PLoS Pathog. 2011 Jul; 7(7):e1002162.

14.     Wang D, Zhang S, Li L, Liu X, Mei K, Wang X*. Structural insights into the assembly and activation of IL-1b with its receptors. Nat. Immunol. 2010, 11: 905-911.

15.     Gui M, W Song, H Zhou, J Xu, S Chen, Y Xiang*, and X Wang*. Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. 2017, Cell Res. 27:119-129.


Contact information

Telephone: +86-10-62789401