Journal
STRUCTURE
Volume 30, Issue 4, Pages 590-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2021.12.011
Keywords
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Funding
- Biomedical Research Council via Agency for Science, Technology, and Research (A*STAR)
- A*STAR [FY21_CF_HTPO SEED_ID_BII_C211418001]
- A*STAR Career Development Fund [C210812031]
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Recent developments in the SARS-CoV-2 pandemic highlight the importance of understanding the allostery in viral proteins for diagnostics and drug design. Allosteric drugs provide a potential solution to avoid escape mutations by inhibiting viral proteins from alternative locations.
Recent developments in the SARS-CoV-2 pandemic point to its inevitable transformation into an endemic disease, urging both refinement of diagnostics for emerging variants of concern (VOCs) and design of variant-specific drugs in addition to vaccine adjustments. Exploring the structure and dynamics of the SARS-CoV-2 Spike protein, we argue that the high-mutability characteristic of RNA viruses coupled with the remarkable flexibility and dynamics of viral proteins result in a substantial involvement of allosteric mechanisms. While allosteric effects of mutations should be considered in predictions and diagnostics of new VOCs, allosteric drugs advantageously avoid escape mutations via non-competitive inhibition originating from alternative distal locations. The exhaustive allosteric signaling and probing maps presented herein provide a comprehensive picture of allostery in the spike protein, making it possible to locate potential mutations that could work as new VOC driversand to determine binding patches that may be targeted by newly developed allosteric drugs.
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