ArticleEMBO reports2009
Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP.
Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- How to Make the CUTiest Sensor in Three Simple Steps for Computational Pedestrians.Methods in molecular biology (Clifton, N.J.) · 2022Article
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- ATP Binding Cassette Transporter A1 is Involved in Extracellular Secretion of Acetylated APE1/Ref-1.International journal of molecular sciences · 2019Article
- A Quantitative Model for cAMP Binding to the Binding Domain of MloK1.Biophysical journal · 2016Article
- Reduced expression of cytochrome oxidases largely explains cAMP inhibition of aerobic growth in Shewanella oneidensis.Scientific reports · 2016Article
- Article
- 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
- 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
- Cyclic dinucleotides bind the C-linker of HCN4 to control channel cAMP responsiveness.Nature chemical biology · 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
- A secondary structural transition in the C-helix promotes gating of cyclic nucleotide-regulated ion channels.The Journal of biological chemistry · 2013Article
- Kinetics of ligand-receptor interaction reveals an induced-fit mode of binding in a cyclic nucleotide-activated protein.Biophysical journal · 2013Article
- Rapid prediction of multi-dimensional NMR data sets.Journal of biomolecular NMR · 2012Article
- Solid-state NMR [13C,15N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel.Biomolecular NMR assignments · 2012Article
- A novel dimerization interface of cyclic nucleotide binding domain, which is disrupted in presence of cAMP: implications for CNG channels gating.Journal of molecular modeling · 2012Article
- Regulation of hyperpolarization-activated cyclic nucleotide-gated (HCN) channel activity by cCMP.The Journal of biological chemistry · 2012Article
- Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
5 authors at 2 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 crucial in neuronal excitability and signal transduction of sensory cells. HCN and CNG channels are activated by binding of cyclic nucleotides to their intracellular cyclic nucleotide-binding domain (CNBD). However, the mechanism by which the binding of cyclic nucleotides opens these channels is not well understood. Here, we report the solution structure of the isolated CNBD of a cyclic nucleotide-sensitive K(+) channel from Mesorhizobium loti. The protein consists of a wide anti-parallel beta-roll topped by a helical bundle comprising five alpha-helices and a short 3(10)-helix. In contrast to the dimeric arrangement ('dimer-of-dimers') in the crystal structure, the solution structure clearly shows a monomeric fold. The monomeric structure of the CNBD supports the hypothesis that the CNBDs transmit the binding signal to the channel pore independently of each other.
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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.