1H, 13C and 15N resonance assignments of SARS-CoV main protease N-terminal domain.

Abstract

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 α-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.

• Authors: Shengnan Zhang, Nan Zhong, Xiaobai Ren, Changwen Jin, Bin Xia
• Journal: Biomolecular NMR assignments (Biomol NMR Assign) Vol. 5 Issue 2 Pg. 143-5 (Oct 2011) ISSN: 1874-270X [Electronic] Netherlands
• PMID: 21181312 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Carbon Isotopes
• Nitrogen Isotopes
• Viral Proteins
• Cysteine Endopeptidases
• Coronavirus 3C Proteases

Topics

• Carbon Isotopes
• Coronavirus 3C Proteases
• Cysteine Endopeptidases (chemistry)
• Nitrogen Isotopes
• Nuclear Magnetic Resonance, Biomolecular
• Severe acute respiratory syndrome-related coronavirus (chemistry)
• Viral Proteins (chemistry)