ArticleScientific reports2020
New Structural insights into Kir channel gating from molecular simulations, HDX-MS and functional studies.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- PIP2-driven cytoplasmic domain motions are coupled to Kir2 channel gating.The Journal of general physiology · 2025Article
- Extended Sampling of Macromolecular Conformations from Uniformly Distributed Points on Multidimensional Normal Mode Hyperspheres.Journal of chemical theory and computation · 2024Article
- Extracellular Kir2.1Circulation research · 2024Article
- Extracellular cysteine disulfide bond break at Cys122 disrupts PIPbioRxiv : the preprint server for biology · 2023Article
- Cryo-electron microscopy unveils unique structural features of the human Kir2.1 channel.Science advances · 2022Article
- Sampling of Protein Conformational Space Using Hybrid Simulations: A Critical Assessment of Recent Methods.Frontiers in molecular biosciences · 2022Article
- Integrative Study of the Structural and Dynamical Properties of a KirBac3.1 Mutant: Functional Implication of a Highly Conserved Tryptophan in the Transmembrane Domain.International journal of molecular sciences · 2021Article
- Insights into the substrate binding mechanism of SULT1A1 through molecular dynamics with excited normal modes simulations.Scientific reports · 2021Article
- Revealing the activation mechanism of autoinhibited RalF by integrated simulation and experimental approaches.Scientific reports · 2021Article
- MicroRNA Biophysically Modulates Cardiac Action Potential by Direct Binding to Ion Channel.Circulation · 2021Article
- Guardians of the Cell: State-of-the-Art of Membrane Proteins from a Computational Point-of-View.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Unexpected Gating Behaviour of an Engineered Potassium Channel Kir.Frontiers in molecular biosciences · 2021Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inward rectifier potassium (Kir) channels play diverse and important roles in shaping action potentials in biological membranes. An increasing number of diseases are now known to be directly associated with abnormal Kir function. However, the gating of Kir still remains unknown. To increase our understanding of its gating mechanism, a dynamical view of the entire channel is essential. Here the gating activation was studied using a recent developped in silico method, MDeNM, which combines normal mode analysis and molecular dynamics simulations that showed for the very first time the importance of interrelated collective and localized conformational movements. In particular, we highlighted the role played by concerted movements of the different regions throughout the entire protein, such as the cytoplasmic and transmembrane domains and the slide helices. In addition, the HDX-MS analysis achieved in these studies provided a comprehensive and detailed view of the dynamics associated with open/closed transition of the Kir channel in coherence with the theoretical results. MDeNM gives access to the probability of the different opening states that are in agreement with our electrophysiological experiments. The investigations presented in this article are important to remedy dysfunctional channels and are of interest for designing new pharmacological compounds.
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