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Article

Conformational changes in protein kinase A along its activation cycle are rooted in the folding energetics of cyclic-nucleotide binding domains.

The Journal of biological chemistry - 1 Jun 2023

Chau Amy K, Bracken Katherine, Bai Lihui, Pham Dominic, Good Lydia L, Maillard Rodrigo A

Abstract excerpt

Cyclic-nucleotide binding (CNB) domains are structurally and evolutionarily conserved signaling modules that regulate proteins with diverse folds and functions. Despite a wealth of structural information, the mechanisms by which CNB domains couple cyclic-nucleotide binding to conformational changes involved in signal transduction remain unknown. Here we combined single-molecule and computational approaches to...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 37150322
DOI: 10.1016/j.jbc.2023.104790
PMCID: PMC10279917

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