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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Takahashi D,Kim Y,Chang KO,Anbanandam A,Prakash Odoi
10.1007/s12104-011-9316-3subject
Has Abstractpub_date
2012-04-01 00:00:00pages
19-21issue
1eissn
1874-2718issn
1874-270Xjournal_volume
6pub_type
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