Agback, Peter
- Department of Molecular Sciences, Swedish University of Agricultural Sciences
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
SLU Authors
Agback, Tatiana
- Department of Molecular Sciences, Swedish University of Agricultural Sciences
- Department of Molecular Sciences, Swedish University of Agricultural Sciences
UKÄ Subject classification
Molecular Biology
Biochemistry
Publication identifier
- DOI: https://doi.org/10.1007/s12104-022-10071-w
Permanent link to this page (URI)
https://res.slu.se/id/publ/116269