Biomolecular NMR Assignments

, Volume 6, Issue 1, pp 19–21

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

Authors

  • Daisuke Takahashi
    • Department of BiochemistryKansas State University
  • Yunjeong Kim
    • Department of Diagnostic Medicine and PathobiologyCollege of Veterinary Medicine, Kansas State University
  • Kyeong-Ok Chang
    • Department of Diagnostic Medicine and PathobiologyCollege of Veterinary Medicine, Kansas State University
  • Asokan Anbanandam
    • Structural Biology CenterThe University of Kansas
    • Department of BiochemistryKansas State University
Article

DOI: 10.1007/s12104-011-9316-3

Cite this article as:
Takahashi, D., Kim, Y., Chang, K. et al. Biomol NMR Assign (2012) 6: 19. doi:10.1007/s12104-011-9316-3

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

NorovirusNorwalk virusViral proteaseNMRResonance assignments

Copyright information

© Springer Science+Business Media B.V. 2011