, Volume 6, Issue 1, pp 19-21
Date: 08 Jun 2011

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

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access


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.