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Research article - Peer-reviewed, 2022

H-1, C-13 and N-15 resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution

Agback, Peter; Lesovoy, Dmitry M.; Han, Xiao; Sun, Renhua; Sandalova, Tatyana; Agback, Tatiana; Achour, Adnane; Orekhov, Vladislav Yu

Abstract

The serotype II Dengue (DENV 2) virus is the most prevalent of all four known serotypes. Herein, we present nearly complete H-1, N-15, and C-13 backbone and H-1, C-13 isoleucine, valine, and leucine methyl resonance assignment of the apo S135A catalytically inactive variant of the DENV 2 protease enzyme folded as a tandem formed between the serine protease domain NS3pro and the cofactor NS2B, as well as the secondary structure prediction of this complex based on the assigned chemical shifts using the TALOS-N software. Our results provide a solid ground for future elucidation of the structure and dynamic of the apo NS3pro/NS2B complex, key for adequate development of inhibitors, and a thorough molecular understanding of their function(s).

Keywords

Dengue 2 virus; NS3 protease; Flavivirus protease; NMR chemical shifts assignment; Methyl assignment; Backbone dynamics

Published in

Biomolecular NMR Assignments
2022, volume: 16, number: 1, pages: 135-145
Publisher: SPRINGER

Authors' information

Swedish University of Agricultural Sciences, Department of Molecular Sciences
Lesovoy, Dmitry M.
Russian Academy of Sciences
Han, Xiao
Karolinska Institutet
Sun, Renhua
Karolinska University Hospital
Sun, Renhua
Karolinska Institutet
Sandalova, Tatyana
Karolinska Institutet
Swedish University of Agricultural Sciences, Department of Molecular Sciences
Achour, Adnane
Karolinska Institutet
Orekhov, Vladislav Yu
University of Gothenburg

UKÄ Subject classification

Biochemistry and Molecular Biology

Publication Identifiers

DOI: https://doi.org/10.1007/s12104-022-10071-w

URI (permanent link to this page)

https://res.slu.se/id/publ/116269