ArticleProceedings of the National Academy of Sciences of the United States of America2006
Voltage sensor conformations in the open and closed states in ROSETTA structural models of K(+) channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.
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141 citing papers in PubMed.
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- The 70-year search for the voltage-sensing mechanism of ion channels.The Journal of physiology · 2022Article
- Nanosecond Pulsed Electric Field (nsPEF): Opening the Biotechnological Pandora's Box.International journal of molecular sciences · 2022Review
- Differential Activation of TRPM8 by the Stereoisomers of Menthol.Frontiers in pharmacology · 2022Article
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- Autism-associated mutations in KProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Chemical modulation of Kv7 potassium channels.RSC medicinal chemistry · 2021Review
- High-Resolution Structures of KHandbook of experimental pharmacology · 2021Article
- Molecular mechanisms underlying menthol binding and activation of TRPM8 ion channel.Nature communications · 2020Article
- Cooperative transport mechanism of human monocarboxylate transporter 2.Nature communications · 2020Article
- Voltage-dependent gating in K channels: experimental results and quantitative models.Pflugers Archiv : European journal of physiology · 2020Review
- Roles for Countercharge in the Voltage Sensor Domain of Ion Channels.Frontiers in pharmacology · 2020Review
- Simulation of Gating Currents of the Shaker K Channel Using a Brownian Model of the Voltage Sensor.Biophysical journal · 2019Article
- Structural mechanisms underlying activation of TRPV1 channels by pungent compounds in gingers.British journal of pharmacology · 2019Article
- Voltage-Dependent Profile Structures of a Kv-Channel via Time-Resolved Neutron Interferometry.Biophysical journal · 2019Article
- Article
- Phosphatidylinositol 4,5-bisphosphate (PIPThe Journal of biological chemistry · 2018Article
- Structural basis for activation of voltage sensor domains in an ion channel TPC1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
81 more citing papers are in PubMed but not listed here.
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3 authors.
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Abstract
Voltage-gated ion channels control generation and propagation of action potentials in excitable cells. Significant progress has been made in understanding structure and function of the voltage-gated ion channels, highlighted by the high-resolution open-state structure of the voltage-gated potassium channel, K(v)1.2. However, because the structure of the closed state is unknown, the gating mechanism remains controversial. We adapted the rosetta membrane method to model the structures of the K(v)1.2 and KvAP channels using homology, de novo, and domain assembly methods and selected the most plausible models using a limited number of experimental constraints. Our model of K(v)1.2 in the open state is very similar in overall topology to the x-ray structure of this channel. Modeling of KvAP in the open state suggests that orientation of the voltage-sensing domain relative to the pore-forming domain is considerably different from the orientation in the K(v)1.2 open state and that the magnitude of the vertical movement of S4 is significantly greater. Structural modeling of closed state of K(v)1.2 suggests gating movement that can be viewed as a sum of two previously suggested mechanisms: translation (2-4 A) plus rotation ( approximately 180 degrees ) of the S4 segment as proposed in the original "sliding helix" or "helical screw" models coupled with a rolling motion of the S1-S3 segments around S4, similar to recent "transporter" models of gating. We propose a unified mechanism of voltage-dependent gating for K(v)1.2 and KvAP in which this major conformational change moves the gating charge across the electric field in an analogous way for both channels.
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