ArticleNature communications2014
Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 64 citations in OpenAlex.
- Structural basis for hyperpolarization-dependent opening of human HCN1 channel.Nature communications · 2024Article
- Structural basis of properties, mechanisms, and channelopathy of cyclic nucleotide-gated channels.Channels (Austin, Tex.) · 2023Review
- Structural Basis for Hyperpolarization-dependent Opening of the Human HCN1 Channel.bioRxiv : the preprint server for biology · 2023Article
- Full opening of helix bundle crossing does not lead to NaK channel activation.The Journal of general physiology · 2022Article
- Objective crystallographic symmetry classifications of a noisy crystal pattern with strong Fedorov-type pseudosymmetries and its optimal image-quality enhancement.Acta crystallographica. Section A, Foundations and advances · 2022Article
- Sample Preparation and Data Collection for Electron Crystallographic Studies on Membrane Protein Structures and Lipid-Protein Interaction.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Single Particle Analysis for High-Resolution 2D Electron Crystallography.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel.Nature structural & molecular biology · 2020Article
- Allosteric conformational change of a cyclic nucleotide-gated ion channel revealed by DEER spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Retrieving high-resolution information from disordered 2D crystals by single-particle cryo-EM.Nature communications · 2019Article
- Article
- An iris diaphragm mechanism to gate a cyclic nucleotide-gated ion channel.Nature communications · 2018Article
- Ligand binding and activation properties of the purified bacterial cyclic nucleotide-gated channel SthK.The Journal of general physiology · 2018Article
- Structural insights into the mechanisms of CNBD channel function.The Journal of general physiology · 2018Review
- The gating mechanism in cyclic nucleotide-gated ion channels.Scientific reports · 2018Article
- Determinants of Isoform-Specific Gating Kinetics of hERG1 Channel: Combined Experimental and Simulation Study.Frontiers in physiology · 2018Article
- Taking the measure of MicroED.Current opinion in structural biology · 2017Review
- Directly watching biomolecules in action by high-speed atomic force microscopy.Biophysical reviews · 2017Review
- Potassium channels in the heart: structure, function and regulation.The Journal of physiology · 2017Review
- A reduced mechanical model for cAMP-modulated gating in HCN channels.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 4 countries.
Funding
Abstract
Cyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly because of a lack of direct structural information. Here we report ligand-induced conformational changes in full-length MloK1, a cyclic nucleotide-modulated potassium channel from the bacterium Mesorhizobium loti, analysed by electron crystallography and atomic force microscopy. Upon cAMP binding, the cyclic nucleotide-binding domains move vertically towards the membrane, and directly contact the S1-S4 voltage sensor domains. This is accompanied by a significant shift and tilt of the voltage sensor domain helices. In both states, the inner pore-lining helices are in an 'open' conformation. We propose a mechanism in which ligand binding can favour pore opening via a direct interaction between the cyclic nucleotide-binding domains and voltage sensors. This offers a simple mechanistic hypothesis for the coupling between ligand gating and voltage sensing in eukaryotic HCN channels.
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