ArticleStructure (London, England : 1993)2012
Mechanism of Cd2+ coordination during slow inactivation in potassium channels.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins.The Journal of membrane biology · 2022Review
- Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores.STAR protocols · 2022Article
- Gating-related Structural Dynamics of the MgtE Magnesium Channel in Membrane-Mimetics Utilizing Site-Directed Tryptophan Fluorescence.Journal of molecular biology · 2021Article
- Computational Analysis of the Crystal and Cryo-EM Structures of P-Loop Channels with Drugs.International journal of molecular sciences · 2021Article
- Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach.Emerging topics in life sciences · 2021Review
- Structural Dynamics of the Paddle Motif Loop in the Activated Conformation of KvAP Voltage Sensor.Biophysical journal · 2020Article
- Biochemical and biophysical characterization of a prokaryotic MgProtein expression and purification · 2019Article
- Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies.Scientific reports · 2019Article
- Prying open a glutamate receptor gate.The Journal of general physiology · 2019Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs.eLife · 2018Article
- Article
- A glimpse into the C-type-inactivated state for a Potassium Channel.Nature structural & molecular biology · 2017Article
- Voltage- and ATP-dependent structural rearrangements of the P2X2 receptor associated with the gating of the pore.The Journal of physiology · 2014Article
- Dynamics transitions at the outer vestibule of the KcsA potassium channel during gating.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Pore helices play a dynamic role as integrators of domain motion during Kv11.1 channel inactivation gating.The Journal of biological chemistry · 2013Article
- C-type inactivation of voltage-gated K+ channels: pore constriction or dilation?The Journal of general physiology · 2013Article
- Inactivation in the potassium channel KcsA.Journal of structural biology: XArticle
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
In K+ channels, rearrangements of the pore outer vestibule have been associated with C-type inactivation gating. Paradoxically, the crystal structure of Open/C-type inactivated KcsA suggests these movements to be modest in magnitude. In this study, we show that under physiological conditions, the KcsA outer vestibule undergoes relatively large dynamic rearrangements upon inactivation. External Cd2+ enhances the rate of C-type inactivation in an cysteine mutant (Y82C) via metal-bridge formation. This effect is not present in a non-inactivating mutant (E71A/Y82C). Tandem dimer and tandem tetramer constructs of equivalent cysteine mutants in KcsA and Shaker K+ channels demonstrate that these Cd2+ metal bridges are formed only between adjacent subunits. This is well supported by molecular dynamics simulations. Based on the crystal structure of Cd2+ -bound Y82C-KcsA in the closed state, together with electron paramagnetic resonance distance measurements in the KcsA outer vestibule, we suggest that subunits must dynamically come in close proximity as the channels undergo inactivation.
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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.