NDLI: The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor.

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The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor.

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The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mo, Lijuan Yang, Haitao Anand, Kanchan Lou, Zhiyong Zhou, Zhe Yang, Maojun Ding, Yi Liu, Yiwei Pang, Hai Bartlam, Mark Gao, George F. Rao, Zihe Ye, Sheng Sun, Lei Hilgenfeld, Rolf
Description	Author Affiliation: Yang H ( Laboratory of Structural Biology, Tsinghua University and National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, 100084 Beijing, China.);
Abstract	A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33.8-kDa protease (also called the 3C-like protease), plays a pivotal role in mediating viral replication and transcription functions through extensive proteolytic processing of two replicase polyproteins, pp1a (486 kDa) and pp1ab (790 kDa). Here, we report the crystal structures of the SARS-CoV main protease at different pH values and in complex with a specific inhibitor. The protease structure has a fold that can be described as an augmented serine-protease, but with a Cys-His at the active site. This series of crystal structures, which is the first, to our knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Endopeptidases Chemistry SARS Virus Enzymology Viral Proteins Amino Acid Chloromethyl Ketones Binding Sites Crystallography, X-Ray Cysteine Cysteine Endopeptidases Glutathione Transferase Histidine Hydrogen-Ion Concentration Models, Chemical Models, Molecular Protein Binding Protein Conformation Protein Structure, Tertiary Substrate Specificity Time Factors Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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