title: Backbone and side-chain ¹H, ¹⁵N, and ¹³C resonance assignments of Norwalk virus protease.
abstract: Norovirus protease cleaves the virus-encoded polyprotein into six mature nonstructural proteins, presenting itself as an essential enzyme for the viral replication as well as an attractive target for the antiviral drug development. A deeper understanding of the structural mechanism of the protease-substrates/inhibitors interactions by means of solution NMR methods would facilitate a rational design of the virus protease inhibitor. We here report the backbone and side-chain resonance assignment of the protease from Norwalk virus, which is the prototype strain of norovirus. The assignment data has been deposited in the BMRB database under the accession number 17523.
authors.affiliation: Department of Biochemistry, Kansas State University, 141 Chalmers Hall, Manhattan, KS 66506, USA.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Takahashi
authors.forename: Yunjeong
authors.initials: Y
authors.lastname: Kim
authors.forename: Kyeong-Ok
authors.initials: KO
authors.lastname: Chang
authors.forename: Asokan
authors.initials: A
authors.lastname: Anbanandam
authors.forename: Om
authors.initials: O
authors.lastname: Prakash
mesh_terms: D000998:Antiviral Agents / Q000737:chemistry / Q000494:pharmacology; D055808:Drug Discovery; D009663:Norwalk virus / Q000187:drug effects / Q000201:enzymology*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D000998:Antiviral Agents; D010447:Peptide Hydrolases