Chemogenetic control of nanobodies
We introduce an engineered nanobody whose affinity to green fluorescent protein (GFP) can be switched on and off with small molecules. By controlling the cellular localization of GFP fusion proteins, the engineered nanobody allows interrogation of their roles in basic biological processes, an approa...
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| Hauptverfasser: | , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
17 February 2020
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| In: |
Nature methods
Year: 2020, Jahrgang: 17, Heft: 3, Pages: 279-282 |
| ISSN: | 1548-7105 |
| DOI: | 10.1038/s41592-020-0746-7 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/s41592-020-0746-7 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/s41592-020-0746-7 |
| Verfasserangaben: | Helen Farrants, Miroslaw Tarnawski, Thorsten G. Müller, Shotaro Otsuka, Julien Hiblot, Birgit Koch, Moritz Kueblbeck, Hans-Georg Kräusslich, Jan Ellenberg and Kai Johnsson |
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| 520 | |a We introduce an engineered nanobody whose affinity to green fluorescent protein (GFP) can be switched on and off with small molecules. By controlling the cellular localization of GFP fusion proteins, the engineered nanobody allows interrogation of their roles in basic biological processes, an approach that should be applicable to numerous previously described GFP fusions. We also outline how the binding affinities of other nanobodies can be controlled by small molecules. | ||
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