Article

Biomolecular NMR Assignments

, Volume 6, Issue 1, pp 19-21

Backbone and side-chain 1H, 15N, and 13C resonance assignments of Norwalk virus protease

  • Daisuke TakahashiAffiliated withDepartment of Biochemistry, Kansas State University
  • , Yunjeong KimAffiliated withDepartment of Diagnostic Medicine and Pathobiology, College of Veterinary Medicine, Kansas State University
  • , Kyeong-Ok ChangAffiliated withDepartment of Diagnostic Medicine and Pathobiology, College of Veterinary Medicine, Kansas State University
  • , Asokan AnbanandamAffiliated withStructural Biology Center, The University of Kansas
  • , Om PrakashAffiliated withDepartment of Biochemistry, Kansas State University Email author 

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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.

Keywords

Norovirus Norwalk virus Viral protease NMR Resonance assignments