ArticleProceedings of the National Academy of Sciences of the United States of America2013
Importance of lipid-pore loop interface for potassium channel structure and function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed.
- Diverse regulation of functional dimerization of a sugar transporter by different interfacial lipids.Nature communications · 2026Article
- MutantMicrobiology spectrum · 2025Article
- Paradoxical SERCA2a Dysregulation Contributes to Atrial Fibrillation in a Model of Diet-Induced Obesity.International journal of molecular sciences · 2025Article
- Mechanism of sensor kinase CitA transmembrane signaling.Nature communications · 2025Article
- Article
- Specific Lipid Studies in Complex Membranes by Solid-State NMR Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V.Nature communications · 2022Article
- Assessing the Role of Lipids in the Molecular Mechanism of Membrane Proteins.International journal of molecular sciences · 2021Review
- Unraveling of a Strongly Correlated Dynamical Network of Residues Controlling the Permeation of Potassium in KcsA Ion Channel.Entropy (Basel, Switzerland) · 2021Article
- KScience advances · 2020Article
- Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Shifts in the selectivity filter dynamics cause modal gating in KNature communications · 2019Article
- Structural and functional characterization of protein-lipid interactions of the Salmonella typhimurium melibiose transporter MelB.BMC biology · 2018Article
- Structure and Dynamics of Membrane Proteins from Solid-State NMR.Annual review of biophysics · 2018Review
- Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms.Nature structural & molecular biology · 2018Article
- Supramolecular Organization and Functional Implications of KAngewandte Chemie (International ed. in English) · 2017Article
- Comparative study of the structure and interaction of the pore helices of the hERG and Kv1.5 potassium channels in model membranes.European biophysics journal : EBJ · 2017Article
- Dynamic Nuclear Polarization Signal Enhancement with High-Affinity Biradical Tags.The journal of physical chemistry. B · 2017Article
- Probing Conformational Changes during the Gating Cycle of a Potassium Channel in Lipid Bilayers.Biophysical journal · 2017Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Potassium (i.e., K(+)) channels allow for the controlled and selective passage of potassium ions across the plasma membrane via a conserved pore domain. In voltage-gated K(+) channels, gating is the result of the coordinated action of two coupled gates: an activation gate at the intracellular entrance of the pore and an inactivation gate at the selectivity filter. By using solid-state NMR structural studies, in combination with electrophysiological experiments and molecular dynamics simulations, we show that the turret region connecting the outer transmembrane helix (transmembrane helix 1) and the pore helix behind the selectivity filter contributes to K(+) channel inactivation and exhibits a remarkable structural plasticity that correlates to K(+) channel inactivation. The transmembrane helix 1 unwinds when the K(+) channel enters the inactivated state and rewinds during the transition to the closed state. In addition to well-characterized changes at the K(+) ion coordination sites, this process is accompanied by conformational changes within the turret region and the pore helix. Further spectroscopic and computational results show that the same channel domain is critically involved in establishing functional contacts between pore domain and the cellular membrane. Taken together, our results suggest that the interaction between the K(+) channel turret region and the lipid bilayer exerts an important influence on the selective passage of potassium ions via the K(+) channel pore.
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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.