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De novo design of tyrosine and serine kinase-driven protein switches

Nat Struct Mol Biol. 2021-09; 
Nicholas B Woodall, Zara Weinberg, Jesslyn Park, Florian Busch, Richard S Johnson, Mikayla J Feldbauer, Michael Murphy, Maggie Ahlrichs, Issa Yousif, Michael J MacCoss, Vicki H Wysocki, Hana El-Samad, David Baker
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摘要

Kinases play central roles in signaling cascades, relaying information from the outside to the inside of mammalian cells. De novo designed protein switches capable of interfacing with tyrosine kinase signaling pathways would open new avenues for controlling cellular behavior, but, so far, no such systems have been described. Here we describe the de novo design of two classes of protein switch that link phosphorylation by tyrosine and serine kinases to protein-protein association. In the first class, protein-protein association is required for phosphorylation by the kinase, while in the second class, kinase activity drives protein-protein association. We design systems that couple protein binding to kinase activ... More

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