ArticleStructure (London, England : 1993)2018
Cork-in-Bottle Occlusion of Fluoride Ion Channels by Crystallization Chaperones.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- The molecular mechanism of fluoride export by the eukaryotic fluoride channel FEX.Nature communications · 2025Article
- The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis.Nature communications · 2024Review
- Dimerization mechanism of an inverted-topology ion channel in membranes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Fluoride permeation mechanism of the Fluc channel in liposomes revealed by solid-state NMR.Science advances · 2023Article
- Controlling ion channel function with renewable recombinant antibodies.The Journal of physiology · 2022Review
- Ion permeation, selectivity, and electronic polarization in fluoride channels.Biophysical journal · 2022Article
- N-terminal Transmembrane-Helix Epitope Tag for X-ray Crystallography and Electron Microscopy of Small Membrane Proteins.Journal of molecular biology · 2021Article
- Article
- Membrane Exporters of Fluoride Ion.Annual review of biochemistry · 2021Review
- The application of Poisson distribution statistics in ion channel reconstitution to determine oligomeric architecture.Methods in enzymology · 2021Article
- Review
- An Interfacial Sodium Ion is an Essential Structural Feature of Fluc Family Fluoride Channels.Journal of molecular biology · 2020Article
- Monobodies as enabling tools for structural and mechanistic biology.Current opinion in structural biology · 2020Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Crystallization of dual-topology fluoride (Fluc) channels requires small, soluble crystallization chaperones known as monobodies, which act as primary crystal lattice contacts. Previous structures of Flucs have been solved in the presence of monobodies that inhibit fluoride currents in single-channel electrophysiological recordings. These structures have revealed two-fold symmetric, doubly bound arrangements, with one monobody on each side of the membrane. The combined electrophysiological and structural observations raise the possibility that chaperone binding allosterically closes the channel, altering the structure from its conducting form. To address this, we identify and solve the structure with a different monobody that only partially blocks fluoride currents. The structure of the channel-monobody complex is asymmetric, with monobody bound to one side of the channel only. The channel conformation is nearly identical on the bound and uncomplexed sides, and to all previously solved structures, providing direct structural evidence that monobody binding does not induce local structural changes.
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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.