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-Structure paper
Title | Eukaryotic Kv channel Shaker inactivates through selectivity filter dilation rather than collapse. |
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Journal, issue, pages | Sci Adv, Vol. 9, Issue 49, Page eadj5539, Year 2023 |
Publish date | Dec 8, 2023 |
Authors | Robyn Stix / Xiao-Feng Tan / Chanhyung Bae / Ana I Fernández-Mariño / Kenton J Swartz / José D Faraldo-Gómez / |
PubMed Abstract | Eukaryotic voltage-gated K channels have been extensively studied, but the structural bases for some of their most salient functional features remain to be established. C-type inactivation, for ...Eukaryotic voltage-gated K channels have been extensively studied, but the structural bases for some of their most salient functional features remain to be established. C-type inactivation, for example, is an auto-inhibitory mechanism that confers temporal resolution to their signal-firing activity. In a recent breakthrough, studies of a mutant of Shaker that is prone to inactivate indicated that this process entails a dilation of the selectivity filter, the narrowest part of the ion conduction pathway. Here, we report an atomic-resolution cryo-electron microscopy structure that demonstrates that the wild-type channel can also adopt this dilated state. All-atom simulations corroborate this conformation is congruent with the electrophysiological characteristics of the C-type inactivated state, namely, residual K conductance and altered ion specificity, and help rationalize why inactivation is accelerated or impeded by certain mutations. In summary, this study establishes the molecular basis for an important self-regulatory mechanism in eukaryotic K channels, laying a solid foundation for further studies. |
External links | Sci Adv / PubMed:38064553 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.39 Å |
Structure data | EMDB-41193, PDB-8teo: |
Chemicals | ChemComp-POV: ChemComp-K: ChemComp-HOH: |
Source |
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Keywords | MEMBRANE PROTEIN / voltage-gated potassium channel |