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J. Peiris, S. Lai, L. Poon, Y. Guan, L. Yam, W. Lim, J. Nicholls, W. Yee, W. Yan, M. Cheung, V. Cheng, K. Chan, D. Tsang, R. Yung, T. Ng, K. Yuen (2003)
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Without its N-Finger , SARS-CoV Main Protease 1 can Form a Novel Dimer through its C-Terminal Domain 2 3
N. Zhong, Shengnan Zhang, Peng Zou, Jiaxuan Chen, X. Kang, Zhe Li, Chao Liang, C. Jin, B. Xia (2008)
Without Its N-Finger, the Main Protease of Severe Acute Respiratory Syndrome Coronavirus Can Form a Novel Dimer through Its C-Terminal DomainJournal of Virology, 82
Haitao Yang, Maojun Yang, Yi Ding, Yiwei Liu, Z. Lou, Zhe Zhou, Lei Sun, L. Mo, S. Ye, H. Pang, G. Gao, K. Anand, M. Bartlam, R. Hilgenfeld, Z. Rao (2003)
The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitorProceedings of the National Academy of Sciences of the United States of America, 100
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Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase*The Journal of Biological Chemistry, 279
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3D domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main proteaseProtein Cell, 1
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X. Xue, Haitao Yang, W. Shen, Qi Zhao, Jun Li, Kailin Yang, Cheng Chen, Yinghua Jin, M. Bartlam, Z. Rao (2006)
Production of Authentic SARS-CoV Mpro with Enhanced Activity: Application as a Novel Tag-cleavage Endopeptidase for Protein OverproductionJournal of Molecular Biology, 366
The main protease (Mpro) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. SARS-CoV Mpro is composed of a catalytic N-terminal domain and an α-helical C-terminal domain linked by a long loop. Even though the N-terminal domain of SARS-CoV Mpro adopts a similar chymotrypsin-like fold as that of piconavirus 3C protease, the extra C-terminal domain is required for SARS-CoV Mpro to be enzymatically active. Here, we reported the NMR assignments of the SARS-CoV Mpro N-terminal domain alone, which are essential for its solution structure determination.
Biomolecular NMR Assignments – Springer Journals
Published: Dec 23, 2010
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