The ability of enzymes to sense signals and respond by changing their structure and activity underlies cellular processes from signaling to metabolic control. While there have been recent advances in the de novo design of enzymes and conformationally switching proteins, combining these to achieve allosteric regulation of enzymatic activity in a fully designed system remains an outstanding challenge. Here, we show that denoising diffusion models enable the design of compact de novo enzymes whose activity can be allosterically activated or repressed by designed protein effectors. Our results establish a general route to allosteric control over a wide range of catalytic and other protein functions.
Shida, A., Wang, K., Choi, H., Pellock, S., Broerman, A., Salike, S., Grubbe, W., Joyce, E., Kang, A., Bera, A. K., Li, X., Pillai, A., Baker, D.
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