ArticlePloS one2015
Structure of the SthK carboxy-terminal region reveals a gating mechanism for cyclic nucleotide-modulated ion channels.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Membrane-forming phospholipids allosterically modulate native-state prolyl isomerization in a CNG channel.Protein science : a publication of the Protein Society · 2025Article
- Domain coupling in allosteric regulation of SthK measured using time-resolved transition metal ion FRET.eLife · 2025Article
- Article
- Ligand-Coupled Conformational Changes in a Cyclic Nucleotide-Gated Ion Channel Revealed by Time-Resolved Transition Metal Ion FRET.bioRxiv : the preprint server for biology · 2024Article
- PIP2 inhibits pore opening of the cyclic nucleotide-gated channel SthK.Nature communications · 2024Article
- cGMP Signaling in Photoreceptor Degeneration.International journal of molecular sciences · 2023Review
- Native Function of the Bacterial Ion Channel SthK in a Sparsely Tethered Lipid Bilayer Membrane Architecture.The journal of physical chemistry. B · 2023Article
- Discrimination between cyclic nucleotides in a cyclic nucleotide-gated ion channel.Nature structural & molecular biology · 2023Article
- Gating intermediates reveal inhibitory role of the voltage sensor in a cyclic nucleotide-modulated ion channel.Nature communications · 2022Article
- Anionic lipids unlock the gates of select ion channels in the pacemaker family.Nature structural & molecular biology · 2022Article
- Allosteric signaling in C-linker and cyclic nucleotide-binding domain of HCN2 channels.Biophysical journal · 2021Article
- Correlating ion channel structure and function.Methods in enzymology · 2021Article
- Prolyl isomerization controls activation kinetics of a cyclic nucleotide-gated ion channel.Nature communications · 2020Article
- Magnesium efflux from Drosophila Kenyon cells is critical for normal and diet-enhanced long-term memory.eLife · 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
- Binding and structural asymmetry governs ligand sensitivity in a cyclic nucleotide-gated ion channel.The Journal of general physiology · 2019Article
- Functional characterization and optimization of a bacterial cyclic nucleotide-gated channel.The Journal of biological chemistry · 2019Article
- The cyclic nucleotide-binding homology domain of the integral membrane protein CNNM mediates dimerization and is required for MgThe Journal of biological chemistry · 2018Article
- Minimal molecular determinants of isoform-specific differences in efficacy in the HCN channel family.The Journal of general physiology · 2018Article
- Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclic nucleotide-sensitive ion channels are molecular pores that open in response to cAMP or cGMP, which are universal second messengers. Binding of a cyclic nucleotide to the carboxyterminal cyclic nucleotide binding domain (CNBD) of these channels is thought to cause a conformational change that promotes channel opening. The C-linker domain, which connects the channel pore to this CNBD, plays an important role in coupling ligand binding to channel opening. Current structural insight into this mechanism mainly derives from X-ray crystal structures of the C-linker/CNBD from hyperpolarization-activated cyclic nucleotide-modulated (HCN) channels. However, these structures reveal little to no conformational changes upon comparison of the ligand-bound and unbound form. In this study, we take advantage of a recently identified prokaryote ion channel, SthK, which has functional properties that strongly resemble cyclic nucleotide-gated (CNG) channels and is activated by cAMP, but not by cGMP. We determined X-ray crystal structures of the C-linker/CNBD of SthK in the presence of cAMP or cGMP. We observe that the structure in complex with cGMP, which is an antagonist, is similar to previously determined HCN channel structures. In contrast, the structure in complex with cAMP, which is an agonist, is in a more open conformation. We observe that the CNBD makes an outward swinging movement, which is accompanied by an opening of the C-linker. This conformation mirrors the open gate structures of the Kv1.2 channel or MthK channel, which suggests that the cAMP-bound C-linker/CNBD from SthK represents an activated conformation. These results provide a structural framework for better understanding cyclic nucleotide modulation of ion channels, including HCN and CNG channels.
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