ArticleEuropean biophysics journal : EBJ2004
KcsA closed and open: modelling and simulation studies.
Article in European biophysics journal : EBJ, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Conduction and Gating Properties of the TRAAK Channel from Molecular Dynamics Simulations with Different Force Fields.Journal of chemical information and modeling · 2020Article
- Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019Article
- Targeted molecular dynamics (TMD) of the full-length KcsA potassium channel: on the role of the cytoplasmic domain in the opening process.Journal of molecular modeling · 2013Article
- Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations.Proteins · 2010Article
- Ion channel gates: comparative analysis of energy barriers.European biophysics journal : EBJ · 2009Article
- The selectivity of K+ ion channels: testing the hypotheses.Biophysical journal · 2008Article
- Cooperative transition between open and closed conformations in potassium channels.PLoS computational biology · 2008Article
- A pore-blocking hydrophobic motif at the cytoplasmic aperture of the closed-state Nav1.7 channel is disrupted by the erythromelalgia-associated F1449V mutation.The Journal of biological chemistry · 2008Article
- A helix-breaking mutation in TRPML3 leads to constitutive activity underlying deafness in the varitint-waddler mouse.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Ion conductance vs. pore gating and selectivity in KcsA channel: modeling achievements and perspectives.Journal of molecular modeling · 2007Article
- Anionic phospholipid interactions with the potassium channel KcsA: simulation studies.Biophysical journal · 2006Article
- Conformational dynamics of the ligand-binding domain of inward rectifier K channels as revealed by molecular dynamics simulations: toward an understanding of Kir channel gating.Biophysical journal · 2005Article
- A model of voltage gating developed using the KvAP channel crystal structure.Biophysical journal · 2004Article
- Filter flexibility and distortion in a bacterial inward rectifier K+ channel: simulation studies of KirBac1.1.Biophysical journal · 2004Article
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Authors and funding
4 authors.
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Abstract
Bacterial homologues of mammalian potassium channels provide structures of two states of a gated K channel. Thus, the crystal structure of KcsA represents a closed state whilst that of MthK represents an open state. Using homology modelling and molecular dynamics simulations we have built a model of the transmembrane domain of KcsA in an open state and have compared its conformational stability with that of the same domain of KcsA in a closed state. Approximate Born energy calculations of monovalent cations within the two KcsA channel states suggest that the intracellular hydrophobic gate in the closed state provides a barrier of height approximately 5 kT to ion permeation, whilst in the open state the barrier is absent. Simulations (10 ns duration) in an octane slab (a simple membrane mimetic) suggest that closed- and open-state models are of comparable conformational stability, both exhibiting conformational drifts of approximately 3.3 A Calpha RMSD relative to the respective starting models. Substantial conformational fluctuations are observed in the intracellular gate region during both simulations (closed state and open state). In the simulation of open-state KcsA, rapid ( < 5 ns) exit of all three K+ ions occurs through the intracellular mouth of the channel. Helix kink and swivel motion is observed at the molecular hinge formed by residue G99 of the M2 helix. This motion is more substantial for the open- than for the closed-state model of the channel.
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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.