Allosteric regulation of kinase activity in living cells
- Department of Pharmacology, Penn State College of Medicine, United States
- Department of Biomedical Engineering, Penn State University, University Park, United States
- Department of Engineering Science and Mechanics, Penn State University, University Park, United States
- Department of Biochemistry & Molecular Biology, Penn State College of Medicine, United States
- Department of Chemistry, Penn State University, University Park, United States
Figures
Figure 1
Domains of kinase protein responsible for the regulation of function.
Figure 2
Various tools used as allosteric regulators.
(A) Allosteric activation of kinase (ERK2 kinase, PDB ID: 4GT3) by uniRapR (PDB ID: 7F2J) domain that binds to small molecule (rapamycin) causing activation of the protein. (B) Allosteric inhibition of kinase (ERK2 kinase, PDB ID: 4GT3) by insertion of an optogenetic control protein, LOV2 (PDB ID: 2V0W), causing conformational change upon irradiation by blue light. (C) Activation of kinase using monobodies (PDB ID: 3RZW).
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Figure 2—source data 1
Source data for Figure 2.
- https://cdn.elifesciences.org/articles/90574/elife-90574-fig2-data1-v1.docx
Figure 3
Sensor proteins used to control function of kinase protein allosterically.
Chemogenetic tools (LightR, LOV2), optogenetic tool (uniRapR, maltose binding protein), and synthetic protein tool (monobody).
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Allosteric regulation of kinase activity in living cells
eLife 12:RP90574.
https://doi.org/10.7554/eLife.90574.4
