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Changes in protein kinase A conformational entropy by ATP-competitive inhibitors

Olivieri, Cristina
Veglia, Gianluigi
2022-05-09
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Persistent link to this item

https://doi.org/10.13020/kswg-6d07
 https://hdl.handle.net/11299/227294
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2014-07-01
2021-11-30

Date completed

2021-12-30

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Title

Changes in protein kinase A conformational entropy by ATP-competitive inhibitors

Published Date

2022-05-09

Authors

Group

University of Minnesota, BMBB Department, Structural Biology Division, Professor Gianluigi Veglia Lab

Author Contact

Veglia, Gianluigi
vegli001@umn.edu

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Experimental Data
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Abstract

NMR characterization of the structural and dynamic changes of the catalytic subunit of cAMP-dependent protein kinase A (PKA-C) in complex with balanol and H89, two ATP-competitive inhibitors. This study aims to unveil how these two inhibitors affect the PKA-C structure and dynamics and how these changes govern the enzyme binding cooperativity and conformational dynamic. These data are part of a paper that has been sent to a peer-review paper.

Description

Proton and Nitrogen chemical shift files from NMR TROSY-HSQC spectra of PKA-C bound to balanol and H89, with or w/t pseudo-substrate peptide (PKI). These list files have been used for chemical shift perturbation (CSP) plots, CHEmical Shift Covariance Analysis (CHESCA), and COordiNate ChemIcal Shift bEhavior (CONCISE) analysis. Correlation scores vs. residue derived from CHESCA analysis for the balanol/ and H89/PKA-C complexes and their correlation with the binding cooperativity coefficient of the enzyme bound to different nucleotide/inhibitors. Calculation of the conformational energy derived from the fast-dynamics of the methyl group side chains of Isoleucine, Leucine, and Valin (ILV) residues of PKA-C bound to nucleotide/inhibitors.

Referenced by

ATP-Competitive Inhibitors Modulate the Substrate Binding Cooperativity of a Kinase by Altering its Conformational Entropy

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License

Attribution-NonCommercial-NoDerivs 3.0 United States
 http://creativecommons.org/licenses/by-nc-nd/3.0/us/

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Data Repository for U of M (DRUM)

Funding information

NIH GM100310 and S10 OD021536 to Gianluigi Veglia

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Suggested citation

Olivieri, Cristina; Veglia, Gianluigi. (2022). Changes in protein kinase A conformational entropy by ATP-competitive inhibitors. Retrieved from the Data Repository for the University of Minnesota (DRUM), https://doi.org/10.13020/kswg-6d07.

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NMR_List_file.xlsx
Proton and Nitrogen chemical shift files from NMR TROSY-HSQC spectra of PKA-C bound to balanol and H89, with or w/t pseudo-substrate peptide (PKI)
(52.71 KB)

Correlation_score.xlsx
Correlation scores vs. residue derived from CHESCA analysis for the balanol/ and H89/PKA-C complexes
(21.09 KB)

Conformational_entropy_CO_051222.xlsx
Calculation of the conformational energy derived from the fast-dynamics of the methyl group side chains of Isoleucine, Leucine, and Valin (ILV) residues of PKA-C bound to nucleotide/inhibitors
(37.88 KB)

PreservationFiles.zip
Preservation format of data files
(125.18 KB)

Readme_Olivieri_20220510.txt
Description of data
(19.36 KB)

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