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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 ?-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.

SUBMITTER: Zhang S

PROVIDER: S-EPMC7091140 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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

Zhang Shengnan S Zhong Nan N Ren Xiaobai X Jin Changwen C Xia Bin B

Biomolecular NMR assignments 20101223 2

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 prote ...[more]

PMID: 21181312

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