ArticleBiophysical journal2004
In silico activation of KcsA K+ channel by lateral forces applied to the C-termini of inner helices.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 27 citations in OpenAlex.
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- Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes.Molecules (Basel, Switzerland) · 2019Review
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- State-dependent inter-repeat contacts of exceptionally conserved asparagines in the inner helices of sodium and calcium channels.Pflugers Archiv : European journal of physiology · 2015Article
- Probing the energy landscape of activation gating of the bacterial potassium channel KcsA.PLoS computational biology · 2013Article
- Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations.Proteins · 2010Article
- Computational analysis of membrane proteins: the largest class of drug targets.Drug discovery today · 2009Review
- Generation, comparison, and merging of pathways between protein conformations: gating in K-channels.Biophysical journal · 2008Article
- Cooperative transition between open and closed conformations in potassium channels.PLoS computational biology · 2008Article
- Desensitization of chemical activation by auxiliary subunits: convergence of molecular determinants critical for augmenting KCNQ1 potassium channels.The Journal of biological chemistry · 2008Article
- End-point targeted molecular dynamics: large-scale conformational changes in potassium channels.Biophysical journal · 2008Article
- Quantum mechanical calculations of charge effects on gating the KcsA channel.Biochimica et biophysica acta · 2007Article
- New roles for a key glycine and its neighboring residue in potassium channel gating.Biophysical journal · 2006Article
- Common mechanism of pore opening shared by five different potassium channels.Biophysical journal · 2006Article
- Investigating the putative glycine hinge in Shaker potassium channel.The Journal of general physiology · 2005Article
- KvAP-based model of the pore region of shaker potassium channel is consistent with cadmium- and ligand-binding experiments.Biophysical journal · 2005Article
- Genetic selection of activatory mutations in KcsA.Channels (Austin, Tex.)Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Crystallographic studies of K(+) channels in the closed (KcsA) and open (MthK) states suggest that Gly(99) (KcsA numbering) in the inner helices serves as a gating hinge during channel activation. However, some P-loop channels have larger residues in the corresponding position. The comparison of x-ray structures of KcsA and MthK shows that channel activation alters backbone torsions and helical H-bonds in residues 95-105. Importantly, the changes in Gly(99) are not the largest ones. This raises questions about the mechanism of conformational changes upon channel gating. In this work, we have built a model of the open KcsA using MthK as a template and simulated opening and closing of KcsA by constraining C-ends of the inner helices at a gradually changing distance from the pore axis without restraining mobility of the helices along the axis. At each imposed distance, the energy was Monte Carlo-minimized. The channel-opening and channel-closing trajectories arrived to the structures in which the backbone geometry was close to that seen in MthK and KcsA, respectively. In the channel-opening trajectory, the constraints-induced lateral forces caused kinks at midpoints of the inner helices between Val(97) and Gly(104) but did not destroy interdomain contacts, the pore helices, and the selectivity filter. The simulated activation of the Gly(99)Ala mutant yielded essentially similar results. Analysis of interresidue energies shows that the N-terminal parts of the inner helices form strong attractive contacts with the pore helices and the outer helices. The lateral forces induce kinks at the position where the helix-breaking torque is maximal and the intersegment contacts vanish. This mechanism may be conserved in different P-loop channels.
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