ArticleThe Journal of biological chemistry2014
Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- An ancestral glutamate receptor mediates cell volume regulation during high KThe Journal of biological chemistry · 2026Article
- Subunit gating resulting from individual protonation events in Kir2 channels.Research square · 2023Article
- Full opening of helix bundle crossing does not lead to NaK channel activation.The Journal of general physiology · 2022Article
- Ion currents through Kir potassium channels are gated by anionic lipids.Nature communications · 2022Article
- Unexpected Gating Behaviour of an Engineered Potassium Channel Kir.Frontiers in molecular biosciences · 2021Article
- The Lipid Activation Mechanism of a Transmembrane Potassium Channel.Journal of the American Chemical Society · 2020Article
- A constricted opening in Kir channels does not impede potassium conduction.Nature communications · 2020Article
- Kir2.2 p.Thr140Met: a genetic susceptibility to sporadic periodic paralysis.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2018Article
- Calcium channel gating.Pflugers Archiv : European journal of physiology · 2018Review
- Cryo-electron microscopy structures and progress toward a dynamic understanding of KThe Journal of general physiology · 2018Review
- Control of Kir channel gating by cytoplasmic domain interface interactions.The Journal of general physiology · 2017Article
- Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.Proteins · 2016Article
- Solution-Based Single-Molecule FRET Studies of K(+) Channel Gating in a Lipid Bilayer.Biophysical journal · 2016Article
- Modular Design of the Selectivity Filter Pore Loop in a Novel Family of Prokaryotic 'Inward Rectifier' (NirBac) channels.Scientific reports · 2015Article
- Structure of potassium channels.Cellular and molecular life sciences : CMLS · 2015Review
- Molecular Dynamics Simulations of KirBac1.1 Mutants Reveal Global Gating Changes of Kir Channels.Journal of chemical information and modeling · 2015Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 4 countries.
Funding
Abstract
KirBac channels are prokaryotic homologs of mammalian inwardly rectifying potassium (Kir) channels, and recent structures of KirBac3.1 have provided important insights into the structural basis of gating in Kir channels. In this study, we demonstrate that KirBac3.1 channel activity is strongly pH-dependent, and we used x-ray crystallography to determine the structural changes that arise from an activatory mutation (S205L) located in the cytoplasmic domain (CTD). This mutation stabilizes a novel energetically favorable open conformation in which changes at the intersubunit interface in the CTD also alter the electrostatic potential of the inner cytoplasmic cavity. These results provide a structural explanation for the activatory effect of this mutation and provide a greater insight into the role of the CTD in Kir channel gating.
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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.