ArticleNature structural & molecular biology2023
Discrimination between cyclic nucleotides in a cyclic nucleotide-gated ion channel.
Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- High-speed atomic force microscopy of membrane proteins: From dynamic imaging to integrative structural biology.Current opinion in structural biology · 2026Review
- Review
- Molecular contacts in self-assembling clusters of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Unique Roles of Ion Channels in Pluripotent Stem Cells in Response to Biological Stimuli.Biology · 2024Review
- AFM Imaging Reveals MicroRNA-132 to be a Positive Regulator of Synaptic Functions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Cyclic nucleotide-gated ion channels are crucial in many physiological processes such as vision and pacemaking in the heart. SthK is a prokaryotic homolog with high sequence and structure similarities to hyperpolarization-activated and cyclic nucleotide-modulated and cyclic nucleotide-gated channels, especially at the level of the cyclic nucleotide binding domains (CNBDs). Functional measurements showed that cyclic adenosine monophosphate (cAMP) is a channel activator while cyclic guanosine monophosphate (cGMP) barely leads to pore opening. Here, using atomic force microscopy single-molecule force spectroscopy and force probe molecular dynamics simulations, we unravel quantitatively and at the atomic level how CNBDs discriminate between cyclic nucleotides. We find that cAMP binds to the SthK CNBD slightly stronger than cGMP and accesses a deep-bound state that a cGMP-bound CNBD cannot reach. We propose that the deep binding of cAMP is the discriminatory state that is essential for cAMP-dependent channel activation.
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Registered trials
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.