ArticleProceedings of the National Academy of Sciences of the United States of America2015
Ion-binding properties of a K+ channel selectivity filter in different conformations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 40 citations in OpenAlex.
- Elucidating the role of lipid interactions in stabilizing the membrane protein KcsA.Biophysical journal · 2024Article
- Article
- Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023Article
- Full opening of helix bundle crossing does not lead to NaK channel activation.The Journal of general physiology · 2022Article
- Cell-Free Expression of Proton-Coupled Folate Transporter in the Presence of Nanodiscs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Structures of Gating Intermediates in a KJournal of molecular biology · 2021Article
- Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.International journal of molecular sciences · 2021Article
- Thermodynamics of ion binding and occupancy in potassium channels.Chemical science · 2021Article
- Unraveling of a Strongly Correlated Dynamical Network of Residues Controlling the Permeation of Potassium in KcsA Ion Channel.Entropy (Basel, Switzerland) · 2021Article
- Impact of nanodisc lipid composition on cell-free expression of proton-coupled folate transporter.PloS one · 2021Article
- Comparison of KHandbook of experimental pharmacology · 2021Article
- KScience advances · 2020Article
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
- Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019Article
- Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies.Scientific reports · 2019Article
- Retrieving high-resolution information from disordered 2D crystals by single-particle cryo-EM.Nature communications · 2019Article
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- Opening leads to closing: Allosteric crosstalk between the activation and inactivation gates in KcsA.The Journal of general physiology · 2018Article
- Rapid constriction of the selectivity filter underlies C-type inactivation in the KcsA potassium channel.The Journal of general physiology · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
K(+) channels are membrane proteins that selectively conduct K(+) ions across lipid bilayers. Many voltage-gated K(+) (KV) channels contain two gates, one at the bundle crossing on the intracellular side of the membrane and another in the selectivity filter. The gate at the bundle crossing is responsible for channel opening in response to a voltage stimulus, whereas the gate at the selectivity filter is responsible for C-type inactivation. Together, these regions determine when the channel conducts ions. The K(+) channel from Streptomyces lividians (KcsA) undergoes an inactivation process that is functionally similar to KV channels, which has led to its use as a practical system to study inactivation. Crystal structures of KcsA channels with an open intracellular gate revealed a selectivity filter in a constricted conformation similar to the structure observed in closed KcsA containing only Na(+) or low [K(+)]. However, recent work using a semisynthetic channel that is unable to adopt a constricted filter but inactivates like WT channels challenges this idea. In this study, we measured the equilibrium ion-binding properties of channels with conductive, inactivated, and constricted filters using isothermal titration calorimetry (ITC). EPR spectroscopy was used to determine the state of the intracellular gate of the channel, which we found can depend on the presence or absence of a lipid bilayer. Overall, we discovered that K(+) ion binding to channels with an inactivated or conductive selectivity filter is different from K(+) ion binding to channels with a constricted filter, suggesting that the structures of these channels are different.
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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.