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Cheng Chen ——Lecturer

Nationality:
China
Phone:
Email:
chengchen@tju.edu.cn
Office:
School of Life Sciences, Tianjin University; 92 Weijin Road, Nankai District
School:
School of Life Sciences
ResearcherID:
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Education Experience
2002-2006 Bachelor of Science Biophysics Nanjing University
2006-2013 Ph. D. Biology Tsinghua University
Professional Experience
2013-now Lecturer Tianjin University
Research Area

Dr. Chen focuses on exploring the functions of critical replicase proteins involved in the pathogenesis of life-threatening pathogens (Cytomegalovirus, Coronaviruses and Enterovirus 71, etc.) employing the structural biology approaches. He also performs structure-based inhibitor design, aiming at developing effective antiviral lead compounds. As shown below, Fig. 1 illustrates the crystal structure of Enterovirus 71 RNA-dependent RNA polymerase in complex with its primer precursor peptide VPg. Fig. 2 depicts the structure of feline infectious peritonitis virus main protease in complex with a structure-based inhibitor N3.

Figure 1. Crystal structure of Enterovirus 71 (EV71) RNA-dependent RNA polymerase (3D) in complex with its primer precursor peptide VPg (PDB entry 4IKA) and alignment with the structure of Cosackievirus B3 (CVB3) 3D-VPg complex (PDB entry 3CDW) and Poliovirus apo 3D (PDB entry 1RDR).

Figure 2. Crystal structure of feline infectious peritonitis virus main protease in complex with a structure-based inhibitor N3 (PDB entry 5EU8).

Honors and Awards
Patents
Highlighted Publications
Yuna Sun#, Yaxin Wang#, Chao Shan#, Cheng Chen, Peng Xu, Mohan Song, Honggang Zhou, Cheng Yang, Wenbo Xu, Pei-Yong Shi, Bo Zhang*, and Zhiyong Lou*, Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase. Journal of virology, 2012, 86(24): 13662-13671.
Cheng Chen#, Yaxin Wang#, Chao Shan#, Yuna Sun, Peng Xu, Honggang Zhou, Cheng Yang, Pei-Yong Shi, Zihe Rao, Bo Zhang*, and Zhiyong Lou*, Crystal structure of enterovirus 71 RNA-dependent RNA polymerase complexed with its protein primer VPg: implication for a trans mechanism of VPg uridylylation. Journal of virology, 2013, 87(10): 5755-5768.
Wang J#, Wang F#, Tan Y, Chen X, Zhao Q, Fu S, Li S*, Chen C*, Yang H. Crystallization and preliminary crystallographic study of Feline infectious peritonitis virus main protease in complex with an inhibitor. Acta Crystallogr F Struct Biol Commun, 2014, 70(Pt 12): 1612-1615.
Xia Chen#, Yusheng Tan#, Fenghua Wang, Jinshan Wang, Qi Zhao, Shuang Li, Sheng Fu*, Cheng Chen*, and Haitao Yang, Expression, crystallization and preliminary crystallographic study of the functional mutant (N60K) of nonstructural protein 9 from Human coronavirus HKU1. Acta crystallographica Section F, Structural biology communications, 2014, 70(12): 1620-1623.
Fenghua Wang#, Cheng Chen#, Xuemeng Liu, Kailin Yang, Xiaoling Xu*, Haitao Yang*. The crystal structure of feline infectious peritonitis virus main protease in complex with synergetic dual inhibitors. J Virol, 2015. (Epub) (#Co-first author, *Corresponding author, same as below)
ResearcherID Publications
Year Title Author(s) Source Volume