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• W4306670540 abstract "Abstract AlphaFold2 (AF2) has revolutionized structural biology by accurately predicting single structures of proteins and protein-protein complexes. However, biological function is rooted in a protein’s ability to sample different conformational substates, and disease-causing point mutations are often due to population changes of these substates. This has sparked immense interest in expanding AF2’s capability to predict conformational substates. We demonstrate that clustering an input multiple sequence alignment (MSA) by sequence similarity enables AF2 to sample alternate states of known metamorphic proteins, including the circadian rhythm protein KaiB, the transcription factor RfaH, and the spindle checkpoint protein Mad2, and score these states with high confidence. Moreover, we use AF2 to identify a minimal set of two point mutations predicted to switch KaiB between its two states. Finally, we used our clustering method, AF-cluster, to screen for alternate states in protein families without known fold-switching, and identified a putative alternate state for the oxidoreductase DsbE. Similarly to KaiB, DsbE is predicted to switch between a thioredoxin-like fold and a novel fold. This prediction is the subject of future experimental testing. Further development of such bioinformatic methods in tandem with experiments will likely have profound impact on predicting protein energy landscapes, essential for shedding light into biological function." @default.
• W4306670540 created "2022-10-19" @default.
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• W4306670540 date "2022-10-17" @default.
• W4306670540 modified "2023-10-18" @default.
• W4306670540 title "Prediction of multiple conformational states by combining sequence clustering with AlphaFold2" @default.
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• W4306670540 doi "https://doi.org/10.1101/2022.10.17.512570" @default.
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