ArticleProceedings of the National Academy of Sciences of the United States of America2019
Identifying coupled clusters of allostery participants through chemical shift perturbations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Gating crosstalk in potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- PHY domain governs structural and photochemical fidelity in the far-red-absorbing state of phytochromes.Frontiers in molecular biosciences · 2026Article
- Dynamic networks connect the USP14 active site region with the proteasome interaction surface.Protein science : a publication of the Protein Society · 2025Article
- Analysis of coordinated NMR chemical shifts to map allosteric regulatory networks in proteins.Methods (San Diego, Calif.) · 2023Article
- Full opening of helix bundle crossing does not lead to NaK channel activation.The Journal of general physiology · 2022Article
- Identification of core allosteric sites through temperature- and nucleus-invariant chemical shift covariance.Biophysical journal · 2022Article
- Ion-dependent structure, dynamics, and allosteric coupling in a non-selective cation channel.Nature communications · 2021Article
- CHESPA/CHESCA-SPARKY: automated NMR data analysis plugins for SPARKY to map protein allostery.Bioinformatics (Oxford, England) · 2021Article
- Informing NMR experiments with molecular dynamics simulations to characterize the dominant activated state of the KcsA ion channel.The Journal of chemical physics · 2021Article
- NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021Article
- Structural Plasticity of the Selectivity Filter in Cation Channels.Frontiers in physiology · 2021Review
- Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Integrated Computational Approaches and Tools forAllosteric Drug Discovery.International journal of molecular sciences · 2020Review
- Use of paramagnetic systems to speed-up NMR data acquisition and for structural and dynamic studies.Solid state nuclear magnetic resonance · 2019Review
- Inactivation in the potassium channel KcsA.Journal of structural biology: XArticle
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Authors and funding
5 authors.
Funding
Abstract
Allosteric couplings underlie many cellular signaling processes and provide an exciting avenue for development of new diagnostics and therapeutics. A general method for identifying important residues in allosteric mechanisms would be very useful, but remains elusive due to the complexity of long-range phenomena. Here, we introduce an NMR method to identify residues involved in allosteric coupling between two ligand-binding sites in a protein, which we call chemical shift detection of allostery participants (CAP). Networks of functional groups responding to each ligand are defined through correlated NMR perturbations. In this process, we also identify allostery participants, groups that respond to both binding events and likely play a role in the coupling between the binding sites. Such residues exhibit multiple functional states with distinct NMR chemical shifts, depending on binding status at both binding sites. Such a strategy was applied to the prototypical ion channel KcsA. We had previously shown that the potassium affinity at the extracellular selectivity filter is strongly dependent on proton binding at the intracellular pH sensor. Here, we analyzed proton and potassium binding networks and identified groups that depend on both proton and potassium binding (allostery participants). These groups are viewed as candidates for transmitting information between functional units. The vital role of one such identified amino acid was validated through site-specific mutagenesis, electrophysiology functional studies, and NMR-detected thermodynamic analysis of allosteric coupling. This strategy for identifying allostery participants is likely to have applications for many other systems.
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