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

doi:10.1007/s12104-011-9316-3

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

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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.

Original language	English
Pages (from-to)	19-21
Number of pages	3
Journal	Biomolecular NMR Assignments
Volume	6
Issue number	1
DOIs	https://doi.org/10.1007/s12104-011-9316-3
Publication status	Published - Apr 2012
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry

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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",

note = "Funding Information: Acknowledgements We would like to thank Drs Thallapuranam Krishnaswamy S. Kumar, Haribabu Arthanari, and Gianluigi Veglia for their supports and discussion with NMR experiments. This work was supported by NIH grants 1S10RR025441, RR17686, RR17708 and U01AI081891, Johnson Center for Basic Cancer Research, and Targeted Excellence Programs of Kansas State University.",

year = "2012",

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doi = "10.1007/s12104-011-9316-3",

language = "English",

volume = "6",

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journal = "Biomolecular NMR Assignments",

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AU - Takahashi, Daisuke

AU - Kim, Yunjeong

AU - Chang, Kyeong Ok

AU - Anbanandam, Asokan

AU - Prakash, Om

N1 - Funding Information: Acknowledgements We would like to thank Drs Thallapuranam Krishnaswamy S. Kumar, Haribabu Arthanari, and Gianluigi Veglia for their supports and discussion with NMR experiments. This work was supported by NIH grants 1S10RR025441, RR17686, RR17708 and U01AI081891, Johnson Center for Basic Cancer Research, and Targeted Excellence Programs of Kansas State University.

PY - 2012/4

Y1 - 2012/4

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.

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

Abstract

All Science Journal Classification (ASJC) codes

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