Publication: Broadening the Utility of Farnesyltransferase-Catalyzed Protein Labeling Using Norbornene-Tetrazine Click Chemistry
Broadening the Utility of Farnesyltransferase-Catalyzed Protein Labeling Using Norbornene-Tetrazine Click Chemistry
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Auger, S. A., Venkatachalapathy, S., Suazo, K. F. G., Wang, Y., Sarkis, A. W., Bernhagen, K., Justyna, K., Schaefer, J. V., Wollack, J. W., Plückthun, A., Li, L., & Distefano, M. D. (2024). Broadening the Utility of Farnesyltransferase-Catalyzed Protein Labeling Using Norbornene-Tetrazine Click Chemistry. Bioconjugate Chemistry, 35(7), 922–933. https://doi.org/10.1021/acs.bioconjchem.4c00072
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Bioorthogonal chemistry has gained widespread use in the study of many biological systems of interest, including protein prenylation. Prenylation is a post-translational modification, in which one or two 15- or 20-carbon isoprenoid chains are transferred onto cysteine residues near the C-terminus of a target protein. The three main enzymes─protein farnesyltransferase (FTase), geranylgeranyl transferase I (GGTase I), and geranylgeranyl transferase II (GGTase II)─that catalyze this process have been shown to tolerate numerous structural
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Auger, S. A., Venkatachalapathy, S., Suazo, K. F. G., Wang, Y., Sarkis, A. W., Bernhagen, K., Justyna, K., Schaefer, J. V., Wollack, J. W., Plückthun, A., Li, L., & Distefano, M. D. (2024). Broadening the Utility of Farnesyltransferase-Catalyzed Protein Labeling Using Norbornene-Tetrazine Click Chemistry. Bioconjugate Chemistry, 35(7), 922–933. https://doi.org/10.1021/acs.bioconjchem.4c00072