Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 5, Issue 2, Pages 143-145Publisher
SPRINGER
DOI: 10.1007/s12104-010-9287-9
Keywords
SARS-CoV; Main protease; N-terminal domain; NMR
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Funding
- 973 Program of China [2003CB514104]
- NSFC [30125009]
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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. SARS-CoV M-pro is composed of a catalytic N-terminal domain and an alpha-helical C-terminal domain linked by a long loop. Even though the N-terminal domain of SARS-CoV M-pro adopts a similar chymotrypsin-like fold as that of piconavirus 3C protease, the extra C-terminal domain is required for SARS-CoV M-pro to be enzymatically active. Here, we reported the NMR assignments of the SARS-CoV M-pro N-terminal domain alone, which are essential for its solution structure determination.
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