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

被引：0
作者：
Daisuke Takahashi
Yunjeong Kim
Kyeong-Ok Chang
Asokan Anbanandam
Om Prakash
机构：
[1] Kansas State University,Department of Biochemistry
[2] College of Veterinary Medicine,Department of Diagnostic Medicine and Pathobiology
[3] Kansas State University,Structural Biology Center
[4] The University of Kansas,undefined
来源：
Biomolecular NMR Assignments | 2012年 / 6卷
关键词：
Norovirus; Norwalk virus; Viral protease; NMR; Resonance assignments;
D O I：
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学科分类号：
摘要：
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.
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页码：19 / 21
页数：2
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