ArticleBiophysical journal2008
Models of voltage-dependent conformational changes in NaChBac channels.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 29 citations in OpenAlex.
- Structural model of the open-closed-inactivated cycle of prokaryotic voltage-gated sodium channels.The Journal of general physiology · 2015Review
- Structure and function of voltage-gated sodium channels at atomic resolution.Experimental physiology · 2014Review
- The conserved phenylalanine in the K+ channel voltage-sensor domain creates a barrier with unidirectional effects.Biophysical journal · 2013Article
- Structural basis for gating charge movement in the voltage sensor of a sodium channel.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The free energy barrier for arginine gating charge translation is altered by mutations in the voltage sensor domain.PloS one · 2012Article
- Molecular dynamics simulations of voltage-gated cation channels: insights on voltage-sensor domain function and modulation.Frontiers in pharmacology · 2012Article
- Gating charge interactions with the S1 segment during activation of a Na+ channel voltage sensor.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- NaChBac: the long lost sodium channel ancestor.Biochemistry · 2011Article
- An electrostatic potassium channel opener targeting the final voltage sensor transition.The Journal of general physiology · 2011Article
- 3₁₀-helix conformation facilitates the transition of a voltage sensor S4 segment toward the down state.Biophysical journal · 2011Article
- Article
- Review
- Coupling between residues on S4 and S1 defines the voltage-sensor resting conformation in NaChBac.Biophysical journal · 2010Article
- Down-state model of the voltage-sensing domain of a potassium channel.Biophysical journal · 2010Article
- The activated state of a sodium channel voltage sensor in a membrane environment.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Symmetry-restrained molecular dynamics simulations improve homology models of potassium channels.Proteins · 2010Article
- Sequential formation of ion pairs during activation of a sodium channel voltage sensor.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Studies of alpha-helicity and intersegmental interactions in voltage-gated Na+ channels: S2D4.PloS one · 2009Article
- Subtype-selective targeting of voltage-gated sodium channels.British journal of pharmacology · 2009Review
- Using a five-state model for fitting amplitude histograms from MaxiK channels: beta-distributions reveal more than expected.European biophysics journal : EBJ · 2009Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Models of the transmembrane region of the NaChBac channel were developed in two open/inactivated and several closed conformations. Homology models of NaChBac were developed using crystal structures of Kv1.2 and a Kv1.2/2.1 chimera as templates for open conformations, and MlotiK and KcsA channels as templates for closed conformations. Multiple molecular-dynamic simulations were performed to refine and evaluate these models. A striking difference between the S4 structures of the Kv1.2-like open models and MlotiK-like closed models is the secondary structure. In the open model, the first part of S4 forms an alpha-helix, and the last part forms a 3(10) helix, whereas in the closed model, the first part of S4 forms a 3(10) helix, and the last part forms an alpha-helix. A conformational change that involves this type of transition in secondary structure should be voltage-dependent. However, this transition alone is not sufficient to account for the large gating charge movement reported for NaChBac channels and for experimental results in other voltage-gated channels. To increase the magnitude of the motion of S4, we developed another model of an open/inactivated conformation, in which S4 is displaced farther outward, and a number of closed models in which S4 is displaced farther inward. A helical screw motion for the alpha-helical part of S4 and a simple axial translation for the 3(10) portion were used to develop models of these additional conformations. In our models, four positively charged residues of S4 moved outwardly during activation, across a transition barrier formed by highly conserved hydrophobic residues on S1, S2, and S3. The S4 movement was coupled to an opening of the activation gate formed by S6 through interactions with the segment linking S4 to S5. Consistencies of our models with experimental studies of NaChBac and K(v) channels are discussed.
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