Without its N - Finger , SARS - CoV Main Protease 1 can Form a Novel Dimer through its C - Terminal Domain
نویسندگان
چکیده
Abbreviations: 17 severe acute respiratory syndrome, SARS; SARS coronavirus, SARS-CoV; main protease, M; 18 wild-type, WT; ethylene glycolbis succinimidylsuccinate, EGS; 1,4-Dithiothreitol, DTT; 19 2,2-dimethyl-2-silapentanesulfonic acid , DSS; mass spectrometry, MS; fast protein liquid 20 chromatography system, FPLC; nuclear magnetic resonance, NMR; heteronuclear 21 single-quantum coherence, HSQC. 22 AC EP TE D Copyright © 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved. J. Virol. doi:10.1128/JVI.02612-07 JVI Accepts, published online ahead of print on 27 February 2008
منابع مشابه
Without its N-finger, the main protease of severe acute respiratory syndrome coronavirus can form a novel dimer through its C-terminal domain.
The main protease (M(pro)) 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. It was found that SARS-CoV M(pro) exists in solution as an equilibrium of both monomeric and dimeric forms, and the dimeric form is the enzy...
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