Novak, J. (2022). Structural modifications introduced by NS2B cofactor binding to the NS3 protease of the Kyasanur forest disease virus [Data set]. https://urn.nsk.hr/urn:nbn:hr:193:208603.
Novak, Jurica. Structural modifications introduced by NS2B cofactor binding to the NS3 protease of the Kyasanur forest disease virus. Odjel za biotehnologiju, 2022. 04 Sep 2024. https://urn.nsk.hr/urn:nbn:hr:193:208603.
Novak, Jurica. 2022. Structural modifications introduced by NS2B cofactor binding to the NS3 protease of the Kyasanur forest disease virus. Odjel za biotehnologiju. https://urn.nsk.hr/urn:nbn:hr:193:208603.
Novak, J. 2022. Structural modifications introduced by NS2B cofactor binding to the NS3 protease of the Kyasanur forest disease virus. Odjel za biotehnologiju. [Online]. [Accessed 04 September 2024]. Available from: https://urn.nsk.hr/urn:nbn:hr:193:208603.
Novak J. Structural modifications introduced by NS2B cofactor binding to the NS3 protease of the Kyasanur forest disease virus. [Internet]. Odjel za biotehnologiju: , HR; 2022, [cited 2024 September 04] Available from: https://urn.nsk.hr/urn:nbn:hr:193:208603.
J. Novak, Structural modifications introduced by NS2B cofactor binding to the NS3 protease of the Kyasanur forest disease virus, Odjel za biotehnologiju, 2022. Accessed on: Sep 04, 2024. Available: https://urn.nsk.hr/urn:nbn:hr:193:208603.
Title (english)
Structural modifications introduced by NS2B cofactor binding to the NS3 protease of the Kyasanur forest disease virus
Author
Jurica Novak Department of Biotechnology, University of Rijeka, Croatia
Collaborator
Shivananda Kandagalla (Researcher) South Ural State University
Scientific / art field, discipline and subdiscipline
NATURAL SCIENCES Chemistry Theoretical Chemistry
Abstract (english)
Kyasanur Forest Disease virus (KFDV), a neglected human pathogenic virus, is a Flavivirus that causes severe hemorrhagic fever in humans. To develop a new antiviral therapy against KFDV, we focused on the nonstructural proteins NS2B and NS3 of KFDV which are responsible for serine protease activity. The structure of the NS2B/NS3 protease of KFDV using AlphaFold was created and molecular dynamics (MD) simulations with and without NS2B cofactor were performed to investigate structural rearrangements due to cofactor binding and to identify alternative allosteric sites. 100 ns MD simulations for the top 4 hit molecules confirmed the stability of the allosteric complexes.
Methods (english)
Detailed protocol used for MD simulation is described in 'Structural modifications introduced by NS2B cofactor binding to the NS3 protease of the Kyasanur forest disease virus', Ticks and Tick-borne Diseases