ArticleScientific reports2012
Architecture of the HCN selectivity filter and control of cation permeation.
Article in Scientific reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Structural determinants of ivabradine block of the open pore of HCN4.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Ion behavior in the selectivity filter of HCN1 channels.Biophysical journal · 2022Article
- Review: HCN Channels in the Heart.Current cardiology reviews · 2022Review
- When Is a Potassium Channel Not a Potassium Channel?Function (Oxford, England) · 2022Article
- HCN channels contribute to the sensitivity of intravenous anesthetics in developmental mice.Oncotarget · 2018Article
- 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
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Hyperpolarization-activated Cyclic Nucleotide-modulated (HCN) channels are similar in structure and function to voltage-gated potassium channels. Sequence similarity and functional analyses suggest that the HCN pore is potassium channel-like, consisting of a selectivity filter and an activation gate at the outer and inner ends, respectively. In GYG-containing potassium channels, the selectivity filter sequence is 'T/S-V/I/L/T-GYG', forming a row of four binding sites through which potassium ions flow. In HCNs, the equivalent residues are 'C-I-GYG', but whether they also form four cation binding sites is not known. Here, we focus on the anomalous filter residue of HCNs, the cysteine located at the inner side of the selectivity filter. In potassium channels, this position is occupied by threonine or serine and forms the fourth and most internal ion binding site of the selectivity filter. We find that this cysteine in HCNs does not contribute to permeation or form a fourth binding site.
Identifiers
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Registered trials
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