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

被引：6

作者：

Takahashi, Daisuke ^{[1
]}

Kim, Yunjeong ^{[2
]}

Chang, Kyeong-Ok ^{[2
]}

Anbanandam, Asokan ^{[3
]}

Prakash, Om ^{[1
]}

机构：

[1] Kansas State Univ, Dept Biochem, Manhattan, KS 66506 USA

[2] Kansas State Univ, Dept Diagnost Med & Pathobiol, Coll Vet Med, Manhattan, KS 66506 USA

[3] Univ Kansas, Struct Biol Ctr, Lawrence, KS 66047 USA

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2012年 / 6卷 / 01期

关键词：

Norovirus; Norwalk virus; Viral protease; NMR; Resonance assignments;

D O I：

10.1007/s12104-011-9316-3

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

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.

引用

页码：19 / 21

页数：3