title: 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.affiliation: Beijing Nuclear Magnetic Resonance Center, Peking University, 100871, Beijing, People's Republic of China.
authors.forename: Shengnan
authors.initials: S
authors.lastname: Zhang
authors.forename: Nan
authors.initials: N
authors.lastname: Zhong
authors.forename: Xiaobai
authors.initials: X
authors.lastname: Ren
authors.forename: Changwen
authors.initials: C
authors.lastname: Jin
authors.forename: Bin
authors.initials: B
authors.lastname: Xia
mesh_terms: D002247:Carbon Isotopes; D000086782:Coronavirus 3C Proteases; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D045473:Severe acute respiratory syndrome-related coronavirus / Q000737:chemistry*; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086782:Coronavirus 3C Proteases