The role of the αC-β4 loop in regulating cooperativity interaction in Protein Kinase A
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2019-06-01
2022-10-01
2022-10-01
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2022-10-31
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Title
The role of the αC-β4 loop in regulating cooperativity interaction in Protein Kinase A
Published Date
2024-02-19
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Veglia, Gianluigi
vegli001@umn.edu
vegli001@umn.edu
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Abstract
This investigation examines the cooperative modulation of Protein Kinase A (PKA) activity by ATP and substrates, with a specialized focus on the enzyme's catalytic subunit (PKA-C), utilizing NMR-restrained molecular dynamics simulations complemented by advanced Markov Model analysis. Herein, we deposit chemical shift datasets for the PKA-C mutant F100A, both in its apo form and in complex with nucleotides and inhibitors, and activity assay data providing a comprehensive insight into the enzyme's allosteric regulation mechanisms.
Description
• Proton and amide chemical shift list files of PKA-C PKA-C mutant F100A in the apo form, ATPgN-, ADP- and ATPgN/PKI-form. The list files were obtained using standard [1H, 15N]-WADE-TROSY-HSQC pulse sequence on uniformly 15N labeled-protein.
• Raw data of the steady-state coupled enzyme assays of F100A mutant using standard PKA-C peptide substrates (Kempite)
Referenced by
https://doi.org/10.1101/2023.09.12.557419
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National Institute of Health GM 100310 to GV
National Institute of Health HL 144130 to GV.
National Institute of Health HL 144130 to GV.
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Suggested citation
Olivieri, Cristina; Veglia, Gianluigi; Veliparambil Subrahmanian, Manu; Wang, Yingjie. (2024). The role of the αC-β4 loop in regulating cooperativity interaction in Protein Kinase A. Retrieved from the Data Repository for the University of Minnesota (DRUM), https://doi.org/10.13020/8f9s-qd79.
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| File View/Open | Description | Size |
|---|---|---|
| Readme_Veglia_2024.txt | Description of data | 9.02 KB |
| Chemical_shift_F100A.xlsx | proton and amide chemical shift values obtained from [1H, 15N]-WADE-TROSY-HSQC experiments on apo, ATPgN-, ADP-, ATPgN/PKI-bound F100A mutant | 58.62 KB |
| CoupleAssay_F100A.xlsx | Steady-state coupled-enzyme assays of PKA-C mutant F100A using Kemptide as substrate | 11.93 KB |
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