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• W4311549938 abstract "We develop integrated co-evolution and dynamic coupling (ICDC) approach to identify, mutate, and assess distal sites to modulate function. We validate the approach first by analyzing the existing mutational fitness data of TEM-1 β-lactamase and show that allosteric positions co-evolved and dynamically coupled with the active site significantly modulate function. We further apply ICDC approach to identify positions and their mutations that can modulate binding affinity in a lectin, cyanovirin-N (CV-N), that selectively binds to dimannose, and predict binding energies of its variants through Adaptive BP-Dock. Computational and experimental analyses reveal that binding enhancing mutants identified by ICDC impact the dynamics of the binding pocket, and show that rigidification of the binding residues compensates for the entropic cost of binding. This work suggests a mechanism by which distal mutations modulate function through dynamic allostery and provides a blueprint to identify candidates for mutagenesis in order to optimize protein function." @default.
• W4311549938 created "2022-12-27" @default.
• W4311549938 creator A5031821234 @default.
• W4311549938 creator A5050815439 @default.
• W4311549938 creator A5050843177 @default.
• W4311549938 creator A5072725379 @default.
• W4311549938 creator A5080858695 @default.
• W4311549938 creator A5082500059 @default.
• W4311549938 creator A5086535057 @default.
• W4311549938 date "2022-12-06" @default.
• W4311549938 modified "2023-10-18" @default.
• W4311549938 title "Design of novel cyanovirin-N variants by modulation of binding dynamics through distal mutations" @default.
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