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• W2891652830 abstract "Nature provides an array of proteins that change conformation in response to light. The discovery of a complementary array of proteins that bind only the light-state or dark-state conformation of their photoactive partner proteins would allow each light-switchable protein to be used as an optogenetic tool to control protein-protein interactions. However, as many photoactive proteins have no known binding partner, the advantages of optogenetic control-precise spatial and temporal resolution-are currently restricted to a few well-defined natural systems. In addition, the affinities and kinetics of native interactions are often suboptimal and are difficult to engineer in the absence of any structural information. We report a phage display strategy using a small scaffold protein that can be used to discover new binding partners for both light and dark states of a given light-switchable protein. We used our approach to generate binding partners that interact specifically with the light state or the dark state conformation of two light-switchable proteins: PYP, a test case for a protein with no known partners, and AsLOV2, a well-characterized protein. We show that these novel light-switchable protein-protein interactions can function in living cells to control subcellular localization processes." @default.
• W2891652830 created "2018-09-27" @default.
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• W2891652830 date "2018-09-11" @default.
• W2891652830 modified "2023-09-26" @default.
• W2891652830 title "Discovering Selective Binders for Photoswitchable Proteins Using Phage Display" @default.
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• W2891652830 doi "https://doi.org/10.1021/acssynbio.8b00123" @default.
• W2891652830 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30203962" @default.
• W2891652830 hasPublicationYear "2018" @default.
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