ArticleProceedings of the National Academy of Sciences of the United States of America2013
Semisynthetic K+ channels show that the constricted conformation of the selectivity filter is not the C-type inactivated state.
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 45 papers.
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Who cites it
45 citing papers in PubMed, 65 citations in OpenAlex.
- A Cost-EffectiveBioengineering (Basel, Switzerland) · 2024Article
- Conformational Dynamic Studies of Prokaryotic Potassium Channels Explored by Homo-FRET Methodologies.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Molecular Events behind the Selectivity and Inactivation Properties of Model NaK-Derived Ion Channels.International journal of molecular sciences · 2022Article
- Structural basis for C-type inactivation in a Shaker family voltage-gated KScience advances · 2022Article
- A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V.Nature communications · 2022Article
- Structures of Gating Intermediates in a KJournal of molecular biology · 2021Article
- Unraveling of a Strongly Correlated Dynamical Network of Residues Controlling the Permeation of Potassium in KcsA Ion Channel.Entropy (Basel, Switzerland) · 2021Article
- Tetraoctylammonium, a Long Chain Quaternary Ammonium Blocker, Promotes a Noncollapsed, Resting-Like Inactivated State in KcsA.International journal of molecular sciences · 2021Article
- High-Resolution Structures of KHandbook of experimental pharmacology · 2021Article
- A unique mechanism of inactivation gating of the Kv channel family member Kv7.1 and its modulation by PIP2 and calmodulin.Science advances · 2020Article
- 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
- KScience advances · 2020Article
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- 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
- Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies.Scientific reports · 2019Article
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- Identifying coupled clusters of allostery participants through chemical shift perturbations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Challenges and advances in atomistic simulations of potassium and sodium ion channel gating and permeation.The Journal of physiology · 2019Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
C-type inactivation of K(+) channels plays a key role in modulating cellular excitability. During C-type inactivation, the selectivity filter of a K(+) channel changes conformation from a conductive to a nonconductive state. Crystal structures of the KcsA channel determined at low K(+) or in the open state revealed a constricted conformation of the selectivity filter, which was proposed to represent the C-type inactivated state. However, structural studies on other K(+) channels do not support the constricted conformation as the C-type inactivated state. In this study, we address whether the constricted conformation of the selectivity filter is in fact the C-type inactivated state. The constricted conformation can be blocked by substituting the first conserved glycine in the selectivity filter with the unnatural amino acid d-Alanine. Protein semisynthesis was used to introduce d-Alanine into the selectivity filters of the KcsA channel and the voltage-gated K(+) channel KvAP. For semisynthesis of the KvAP channel, we developed a modular approach in which chemical synthesis is limited to the selectivity filter whereas the rest of the protein is obtained by recombinant means. Using the semisynthetic KcsA and KvAP channels, we show that blocking the constricted conformation of the selectivity filter does not prevent inactivation, which suggests that the constricted conformation is not the C-type inactivated state.
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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.