ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- A cAMP Sensor Based on Ligand-Dependent Protein Stabilization.ACS chemical biology · 2022Article
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- The gating mechanism in cyclic nucleotide-gated ion channels.Scientific reports · 2018Article
- Structural Heterogeneity of CNGA1 Channels Revealed by Electrophysiology and Single-Molecule Force Spectroscopy.ACS omega · 2016Article
- Structure and dynamics underlying elementary ligand binding events in human pacemaking channels.eLife · 2016Article
- 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
- Article
- Article
- Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy.Nature communications · 2015Article
- Inherited macular degeneration-associated mutations in CNGB3 increase the ligand sensitivity and spontaneous open probability of cone cyclic nucleotide-gated channels.Frontiers in physiology · 2015Article
- Structure of the SthK carboxy-terminal region reveals a gating mechanism for cyclic nucleotide-modulated ion channels.PloS one · 2015Article
- Structure, dynamics and implied gating mechanism of a human cyclic nucleotide-gated channel.PLoS computational biology · 2014Article
- Structural basis for the mutual antagonism of cAMP and TRIP8b in regulating HCN channel function.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A mechanism for the auto-inhibition of hyperpolarization-activated cyclic nucleotide-gated (HCN) channel opening and its relief by cAMP.The Journal of biological chemistry · 2014Article
- Double electron-electron resonance reveals cAMP-induced conformational change in HCN channels.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 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
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are activated by binding of ligands to a domain (CNBD) located on the cytoplasmic side of the channel. The underlying mechanisms are not well understood. To elucidate the gating mechanism, structures of both the ligand-free and -bound CNBD are required. Several crystal structures of the CNBD from HCN2 and a bacterial CNG channel (MloK1) have been solved. However, for HCN2, the cAMP-free and -bound state did not reveal substantial structural rearrangements. For MloK1, structural information for the cAMP-free state has only been gained from mutant CNBDs. Moreover, in the crystal, the CNBD molecules form an interface between dimers, proposed to be important for allosteric channel gating. Here, we have determined the solution structure by NMR spectroscopy of the cAMP-free wild-type CNBD of MloK1. A comparison of the solution structure of cAMP-free and -bound states reveals large conformational rearrangement on ligand binding. The two structures provide insights on a unique set of conformational events that accompany gating within the ligand-binding site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.