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 Takahashi
  • Yunjeong Kim
  • Kyeong-Ok Chang
  • Asokan Anbanandam
  • Om Prakash
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

Authors and Affiliations

  • Daisuke Takahashi
    • 1
  • Yunjeong Kim
    • 2
  • Kyeong-Ok Chang
    • 2
  • Asokan Anbanandam
    • 3
  • Om Prakash
    • 1
  1. 1.Department of BiochemistryKansas State UniversityManhattanUSA
  2. 2.Department of Diagnostic Medicine and PathobiologyCollege of Veterinary Medicine, Kansas State UniversityManhattanUSA
  3. 3.Structural Biology CenterThe University of KansasLawrenceUSA