ArticleInternational journal of molecular sciences2019
Formation Mechanism of Ion Channel in Channelrhodopsin-2: Molecular Dynamics Simulation and Steering Molecular Dynamics Simulations.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Pore-Opening and Ion-Conduction Mechanism in Channelrhodopsins C1C2, ChR2, and iChloC by Computational Electrophysiology and Constant-pH Simulations.Journal of chemical information and modeling · 2025Article
- Liquid-Liquid Phase Separation Associated with Intrinsically Disordered Proteins: Experimental and Computational Tools.Current protein & peptide science · 2025Review
- Optogenetics: Illuminating the Future of Hearing Restoration and Understanding Auditory Perception.Current gene therapy · 2024Review
- The short-term plasticity of VIP interneurons in motor cortex.Frontiers in synaptic neuroscience · 2024Article
- The Mechanism of the Channel Opening in Channelrhodopsin-2: A Molecular Dynamics Simulation.International journal of molecular sciences · 2023Article
- Time-resolved photoacoustics of channelrhodopsins: early energetics and light-driven volume changes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide.Communications chemistry · 2022Article
- Modeling theRSC advances · 2022Article
- Molecular Dynamics Simulations in Designing DARPins as Phosphorylation-Specific Protein Binders of ERK2.Molecules (Basel, Switzerland) · 2021Article
- The effect on ion channel of different protonation states of E90 in channelrhodopsin-2: a molecular dynamics simulation.RSC advances · 2021Article
- Molecular Dynamics Simulation of Transmembrane Transport of Chloride Ions in Mutants of Channelrhodopsin.Biomolecules · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Channelrhodopsin-2 (ChR2) is a light-activated and non-selective cationic channel protein that can be easily expressed in specific neurons to control neuronal activity by light. Although ChR2 has been extensively used as an optogenetic tool in neuroscience research, the molecular mechanism of cation channel formation following retinal photoisomerization in ChR2 is not well understood. In this paper, studies of the closed and opened state ChR2 structures are presented. The formation of the cationic channel is elucidated in atomic detail using molecular dynamics simulations on the all-trans-retinal (ChR2-trans) configuration of ChR2 and its isomerization products, 13-cis-retinal (ChR2-cis) configuration, respectively. Photoisomerization of the retinal-chromophore causes the destruction of interactions among the crucial residues (e.g., E90, E82, N258, and R268) around the channel and the extended H-bond network mediated by numerous water molecules, which opens the pore. Steering molecular dynamics (SMD) simulations show that the electrostatic interactions at the binding sites in intracellular gate (ICG) and central gate (CG) can influence the transmembrane transport of Na
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