Mechanisms of allostery at the viral surface through the eyes of molecular simulation

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Mechanisms of allostery at the viral surface through the eyes of molecular simulation
Title:
Mechanisms of allostery at the viral surface through the eyes of molecular simulation
Journal Title:
Current Opinion in Structural Biology
Keywords:
Publication Date:
23 December 2023
Citation:
Samsudin, F., Zuzic, L., Marzinek, J. K., & Bond, P. J. (2024). Mechanisms of allostery at the viral surface through the eyes of molecular simulation. Current Opinion in Structural Biology, 84, 102761. https://doi.org/10.1016/j.sbi.2023.102761
Abstract:
The outermost surface layer of any virus is formed by either a capsid shell or envelope. Such layers have traditionally been thought of as immovable structures, but it is becoming apparent that they cannot be viewed exclusively as static architectures protecting the viral genome. A limited number of proteins on the virion surface must perform a multitude of functions in order to orchestrate the viral life cycle, and allostery can regulate their structures at multiple levels of organization, spanning individual molecules, protomers, large oligomeric assemblies, or entire viral surfaces. Here, we review recent contributions from the molecular simulation field to viral surface allostery, with a particular focus on the trimeric spike glycoprotein emerging from the coronavirus surface, and the icosahedral flaviviral envelope complex. As emerging viral pathogens continue to pose a global threat, an improved understanding of viral dynamics and allosteric regulation will prove crucial in developing novel therapeutic strategies.
License type:
Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
Funding Info:
This research / project is supported by the A*STAR - A*STAR AME Young Individual Research Grant (YIRG)
Grant Reference no. : A2084c0160

This research / project is supported by the A*STAR - A*STAR AME Young Individual Research Grant (YIRG)
Grant Reference no. : A2084c0159

This research / project is supported by the A*STAR - ID HTPO Seed Fund
Grant Reference no. : C211418001

This research / project is supported by the National Research Foundation (NRF) - Competitive Research Programme (CRP)
Grant Reference no. : NRF2017NRF-CRP001-027

Lundbeck Foundation Experiment (R346-2020-1944) research grant
Description:
ISSN:
0959-440X
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