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

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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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Keywords

Chemical shift

Protein kinase A

Conformational dynamics

order parameters

ATP-competitive inhibitors

Binding cooperativity

Collection period

2014-07-01
2021-11-30

Date completed

2021-12-30

Date updated

Time period coverage

Geographic coverage

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Journal Title

Journal ISSN

Volume Title

Title

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

Published Date

2022-05-09

Authors

Olivieri, Cristina

Veglia, Gianluigi

Group

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

Author Contact

Veglia, Gianluigi
vegli001@umn.edu

Type

Dataset
Experimental Data
Other Dataset

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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Collections

Data Repository for U of M (DRUM)

Funding information

NIH GM100310 and S10 OD021536 to Gianluigi Veglia

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Previously Published Citation

Suggested citation

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

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