| Autor: |
Cunningham-Bryant D, Dieter EM, Foight GW, Rose JC, Loutey DE, Maly DJ |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of the American Chemical Society [J Am Chem Soc] 2019 Feb 27; Vol. 141 (8), pp. 3352-3355. Date of Electronic Publication: 2019 Feb 14. |
| DOI: |
10.1021/jacs.8b12382 |
| Abstrakt: |
Chemical methods that allow the spatial proximity of proteins to be temporally modulated are powerful tools for studying biology and engineering synthetic cellular behaviors. Here, we describe a new chemically controlled method for rapidly disrupting the interaction between two basally colocalized protein binding partners. Our chemically disrupted proximity (CDP) system is based on the interaction between the hepatitis C virus protease (HCVp) NS3a and a genetically encoded peptide inhibitor. Using clinically approved antiviral inhibitors as chemical disrupters of the NS3a/peptide interaction, we demonstrate that our CDP system can be used to confer temporal control over diverse intracellular processes. This NS3a-based CDP system represents a new modality for engineering chemical control over intracellular protein function that is complementary to currently available techniques. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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