ArticleThe Journal of biological chemistry2013
Pore helices play a dynamic role as integrators of domain motion during Kv11.1 channel inactivation gating.
Article in The Journal of biological chemistry, 2013. 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.
- Dynamical Nonequilibrium Molecular Dynamics Simulations Reveal Atomistic Steps of C-Type Inactivation in Cardiac hERG Channels.Journal of the American Chemical Society · 2026Article
- Article
- Potassium dependent structural changes in the selectivity filter of HERG potassium channels.Nature communications · 2024Article
- Noncanonical electromechanical coupling paths in cardiac hERG potassium channel.Nature communications · 2023Article
- Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structures Illuminate Cardiac Ion Channel Functions in Health and in Long QT Syndrome.Frontiers in pharmacology · 2020Review
- Functional and pharmacological characterization of an S5 domain hERG mutation associated with short QT syndrome.Heliyon · 2019Article
- Determinants of Isoform-Specific Gating Kinetics of hERG1 Channel: Combined Experimental and Simulation Study.Frontiers in physiology · 2018Article
- The S1 helix critically regulates the finely tuned gating of Kv11.1 channels.The Journal of biological chemistry · 2017Article
- Rescue of protein expression defects may not be enough to abolish the pro-arrhythmic phenotype of long QT type 2 mutations.The Journal of physiology · 2016Article
- Getting to the heart of hERG K(+) channel gating.The Journal of physiology · 2015Review
- Cooperative subunit interactions mediate fast C-type inactivation of hERG1 K+ channels.The Journal of physiology · 2014Article
- Role of the cytoplasmic N-terminal Cap and Per-Arnt-Sim (PAS) domain in trafficking and stabilization of Kv11.1 channels.The Journal of biological chemistry · 2014Article
- Hydrophobic interactions between the voltage sensor and pore mediate inactivation in Kv11.1 channels.The Journal of general physiology · 2013Article
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Authors and funding
3 authors.
Funding
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Abstract
Proteins that form ion-selective pores in the membrane of cells are integral to many rapid signaling processes, including regulating the rhythm of the heartbeat. In potassium channels, the selectivity filter is critical for both endowing an exquisite selectivity for potassium ions, as well as for controlling the flow of ions through the pore. Subtle rearrangements in the complex hydrogen-bond network that link the selectivity filter to the surrounding pore helices differentiate conducting (open) from nonconducting (inactivated) conformations of the channel. Recent studies suggest that beyond the selectivity filter, inactivation involves widespread rearrangements of the channel protein. Here, we use rate equilibrium free energy relationship analysis to probe the structural changes that occur during selectivity filter gating in Kv11.1 channels, at near atomic resolution. We show that the pore helix plays a crucial dynamic role as a bidirectional interface during selectivity filter gating. We also define the molecular bases of the energetic coupling between the pore helix and outer helix of the pore domain that occurs early in the transition from open to inactivated states, as well as the coupling between the pore helix and inner helix late in the transition. Our data demonstrate that the pore helices are more than just static structural elements supporting the integrity of the selectivity filter; instead they play a crucial dynamic role during selectivity filter gating.
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