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

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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.

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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.

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Correspondence to Om Prakash.

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Takahashi, D., Kim, Y., Chang, KO. et al. Backbone and side-chain 1H, 15N, and 13C resonance assignments of Norwalk virus protease. Biomol NMR Assign 6, 19–21 (2012). https://doi.org/10.1007/s12104-011-9316-3

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  • DOI: https://doi.org/10.1007/s12104-011-9316-3

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