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

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)19-21
Number of pages3
JournalBiomolecular NMR Assignments
Issue number1
Publication statusPublished - Apr 2012
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

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