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

研究成果: ジャーナルへの寄稿記事

5 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)19-21
ページ数3
ジャーナルBiomolecular NMR Assignments
6
発行部数1
DOI
出版物ステータス出版済み - 4 1 2012
外部発表Yes

Fingerprint

Norwalk virus
Norovirus
Protease Inhibitors
Viruses
Peptide Hydrolases
Polyproteins
Antiviral Agents
Databases
Enzymes
Nuclear magnetic resonance
Proteins
Substrates

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

これを引用

Backbone and side-chain 1H, 15N, and 13C resonance assignments of Norwalk virus protease. / Takahashi, Daisuke; Kim, Yunjeong; Chang, Kyeong Ok; Anbanandam, Asokan; Prakash, Om.

:: Biomolecular NMR Assignments, 巻 6, 番号 1, 01.04.2012, p. 19-21.

研究成果: ジャーナルへの寄稿記事

Takahashi, Daisuke ; Kim, Yunjeong ; Chang, Kyeong Ok ; Anbanandam, Asokan ; Prakash, Om. / Backbone and side-chain 1H, 15N, and 13C resonance assignments of Norwalk virus protease. :: Biomolecular NMR Assignments. 2012 ; 巻 6, 番号 1. pp. 19-21.
@article{f9a18a4fa1024b31a43d491fc73eede0,
title = "Backbone and side-chain 1H, 15N, and 13C resonance assignments of Norwalk virus protease",
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.",
author = "Daisuke Takahashi and Yunjeong Kim and Chang, {Kyeong Ok} and Asokan Anbanandam and Om Prakash",
year = "2012",
month = "4",
day = "1",
doi = "10.1007/s12104-011-9316-3",
language = "English",
volume = "6",
pages = "19--21",
journal = "Biomolecular NMR Assignments",
issn = "1874-2718",
publisher = "Springer Netherlands",
number = "1",

}

TY - JOUR

T1 - Backbone and side-chain 1H, 15N, and 13C resonance assignments of Norwalk virus protease

AU - Takahashi, Daisuke

AU - Kim, Yunjeong

AU - Chang, Kyeong Ok

AU - Anbanandam, Asokan

AU - Prakash, Om

PY - 2012/4/1

Y1 - 2012/4/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84858295982&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84858295982&partnerID=8YFLogxK

U2 - 10.1007/s12104-011-9316-3

DO - 10.1007/s12104-011-9316-3

M3 - Article

C2 - 21647610

AN - SCOPUS:84858295982

VL - 6

SP - 19

EP - 21

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

SN - 1874-2718

IS - 1

ER -