ArticleProceedings of the National Academy of Sciences of the United States of America2011
Cysteine scanning and modification reveal major differences between BK channels and Kv channels in the inner pore region.
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 62 papers.
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Who cites it
62 citing papers in PubMed.
- Lipid gating of BK channels and activation mechanism by negatively charged lipids.Communications chemistry · 2026Article
- Article
- Dibenzoylmethane, a novel β-diketone pore blocker of large-conductance calcium-activated potassium channel.bioRxiv : the preprint server for biology · 2026Article
- Article
- Incorporating physics to overcome data scarcity in predictive modeling of protein function: A case study of BK channels.PLoS computational biology · 2023Article
- Incorporating physics to overcome data scarcity in predictive modeling of protein function: a case study of BK channels.bioRxiv : the preprint server for biology · 2023Article
- Inner pore hydration free energy controls the activation of big potassium channels.Biophysical journal · 2023Article
- BK Channel Gating Mechanisms: Progresses Toward a Better Understanding of Variants Linked Neurological Diseases.Frontiers in physiology · 2021Review
- Calcium-Activated KHandbook of experimental pharmacology · 2021Article
- Selectivity filter ion binding affinity determines inactivation in a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Hydrophobic dewetting in gating and regulation of transmembrane protein ion channels.The Journal of chemical physics · 2020Review
- The action of a BK channel opener.The Journal of general physiology · 2020Article
- Article
- The functionally relevant site for paxilline inhibition of BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Large-conductance CaProceedings of the National Academy of Sciences of the United States of America · 2019Article
- A pharmacological master key mechanism that unlocks the selectivity filter gate in KScience (New York, N.Y.) · 2019Article
- Hydrophobic gating in BK channels.Nature communications · 2018Article
- Threading the biophysics of mammalian Slo1 channels onto structures of an invertebrate Slo1 channel.The Journal of general physiology · 2017Review
2 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
BK channels are regulated by two distinct physiological signals, transmembrane potential and intracellular Ca(2+), each acting through independent modular sensor domains. However, despite a presumably central role in the coupling of sensor activation to channel gating, the pore-lining S6 transmembrane segment has not been systematically studied. Here, cysteine substitution and modification studies of the BK S6 point to substantial differences between BK and Kv channels in the structure and function of the S6-lined inner pore. Gating shifts caused by introduction of cysteines define a pattern and direction of free energy changes in BK S6 distinct from Shaker. Modification of BK S6 residues identifies pore-facing residues that occur at different linear positions along aligned BK and Kv S6 segments. Periodicity analysis suggests that one factor contributing to these differences may be a disruption of the BK S6 α-helix from the unique diglycine motif at the position of the Kv hinge glycine. State-dependent MTS accessibility reveals that, even in closed states, modification can occur. Furthermore, the inner pore of BK channels is much larger than that of K(+) channels with solved crystal structures. The results suggest caution in the use of Kv channel structures as templates for BK homology models, at least in the pore-gate domain.
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