ArticleBiophysical journal2013
Kinetics of ligand-receptor interaction reveals an induced-fit mode of binding in a cyclic nucleotide-activated protein.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
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- Measurement of Kinetics and Active Site Distances in Metalloenzymes Using Paramagnetic NMR withThe journal of physical chemistry letters · 2018Article
- Label-free NMR-based dissociation kinetics determination.Journal of biomolecular NMR · 2017Article
- Characterization of Chemical Exchange Using Relaxation Dispersion of Hyperpolarized Nuclear Spins.Analytical chemistry · 2017Article
- A Quantitative Model for cAMP Binding to the Binding Domain of MloK1.Biophysical journal · 2016Article
- Real-time visualization of conformational changes within single MloK1 cyclic nucleotide-modulated channels.Nature communications · 2016Article
- How to Distinguish Conformational Selection and Induced Fit Based on Chemical Relaxation Rates.PLoS computational biology · 2016Article
- Discrimination between conformational selection and induced fit protein-ligand binding using Integrated Global Fit analysis.European biophysics journal : EBJ · 2016Article
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- Conformational selection in protein binding and function.Protein science : a publication of the Protein Society · 2014Review
- Determinants of ligand selectivity in a cyclic nucleotide-regulated potassium channel.The Journal of general physiology · 2014Article
- A KcsA/MloK1 chimeric ion channel has lipid-dependent ligand-binding energetics.The Journal of biological chemistry · 2014Article
- Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1.Nature communications · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many receptors and ion channels are activated by ligands. One key question concerns the binding mechanism. Does the ligand induce conformational changes in the protein via the induced-fit mechanism? Or does the protein preexist as an ensemble of conformers and the ligand selects the most complementary one, via the conformational selection mechanism? Here, we study ligand binding of a tetrameric cyclic nucleotide-gated channel from Mesorhizobium loti and of its monomeric binding domain (CNBD) using rapid mixing, mutagenesis, and structure-based computational biology. Association rate constants of ∼10(7) M(-1) s(-1) are compatible with diffusion-limited binding. Ligand binding to the full-length CNG channel and the isolated CNBD differ, revealing allosteric control of the CNBD by the effector domain. Finally, mutagenesis of allosteric residues affects only the dissociation rate constant, suggesting that binding follows the induced-fit mechanism. This study illustrates the strength of combining mutational, kinetic, and computational approaches to unravel important mechanistic features of ligand binding.
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