ArticlePLoS computational biology2013
Probing the energy landscape of activation gating of the bacterial potassium channel KcsA.
Article in PLoS computational biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Pressure-tolerant Evolution in Rhodopsin of Deep-diving Whales.Genome biology and evolution · 2026Article
- Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023Article
- The Role of ICL1 and H8 in Class B1 GPCRs; Implications for Receptor Activation.Frontiers in endocrinology · 2021Article
- 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
- Rapid constriction of the selectivity filter underlies C-type inactivation in the KcsA potassium channel.The Journal of general physiology · 2018Article
- Effects of protein-protein interactions and ligand binding on the ion permeation in KCNQ1 potassium channel.PloS one · 2018Article
- Receptor activity-modifying protein dependent and independent activation mechanisms in the coupling of calcitonin gene-related peptide and adrenomedullin receptors to Gs.Biochemical pharmacology · 2017Article
- Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids.The Journal of general physiology · 2016Article
- Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.The Journal of general physiology · 2016Article
- Drug trapping in hERG KMedChemComm · 2016Article
- Molecular Dynamics Simulations of KirBac1.1 Mutants Reveal Global Gating Changes of Kir Channels.Journal of chemical information and modeling · 2015Article
- Inactivation in the potassium channel KcsA.Journal of structural biology: XArticle
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3 authors.
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Abstract
The bacterial potassium channel KcsA, which has been crystallized in several conformations, offers an ideal model to investigate activation gating of ion channels. In this study, essential dynamics simulations are applied to obtain insights into the transition pathways and the energy profile of KcsA pore gating. In agreement with previous hypotheses, our simulations reveal a two phasic activation gating process. In the first phase, local structural rearrangements in TM2 are observed leading to an intermediate channel conformation, followed by large structural rearrangements leading to full opening of KcsA. Conformational changes of a highly conserved phenylalanine, F114, at the bundle crossing region are crucial for the transition from a closed to an intermediate state. 3.9 µs umbrella sampling calculations reveal that there are two well-defined energy barriers dividing closed, intermediate, and open channel states. In agreement with mutational studies, the closed state was found to be energetically more favorable compared to the open state. Further, the simulations provide new insights into the dynamical coupling effects of F103 between the activation gate and the selectivity filter. Investigations on individual subunits support cooperativity of subunits during activation gating.
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