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TitleInactivation of the Kv2.1 channel through electromechanical coupling.
Journal, issue, pagesNature, Vol. 622, Issue 7982, Page 410-417, Year 2023
Publish dateSep 27, 2023
AuthorsAna I Fernández-Mariño / Xiao-Feng Tan / Chanhyung Bae / Kate Huffer / Jiansen Jiang / Kenton J Swartz /
PubMed AbstractThe Kv2.1 voltage-activated potassium (Kv) channel is a prominent delayed-rectifier Kv channel in the mammalian central nervous system, where its mechanisms of activation and inactivation are ...The Kv2.1 voltage-activated potassium (Kv) channel is a prominent delayed-rectifier Kv channel in the mammalian central nervous system, where its mechanisms of activation and inactivation are critical for regulating intrinsic neuronal excitability. Here we present structures of the Kv2.1 channel in a lipid environment using cryo-electron microscopy to provide a framework for exploring its functional mechanisms and how mutations causing epileptic encephalopathies alter channel activity. By studying a series of disease-causing mutations, we identified one that illuminates a hydrophobic coupling nexus near the internal end of the pore that is critical for inactivation. Both functional and structural studies reveal that inactivation in Kv2.1 results from dynamic alterations in electromechanical coupling to reposition pore-lining S6 helices and close the internal pore. Consideration of these findings along with available structures for other Kv channels, as well as voltage-activated sodium and calcium channels, suggests that related mechanisms of inactivation are conserved in voltage-activated cation channels and likely to be engaged by widely used therapeutics to achieve state-dependent regulation of channel activity.
External linksNature / PubMed:37758949 / PubMed Central
MethodsEM (single particle)
Resolution2.95 - 3.32 Å
Structure data

40349

8sd3

EMDB-40349, PDB-8sd3:
CryoEM structure of rat Kv2.1(1-598) wild type in nanodiscs
Method: EM (single particle) / Resolution: 2.95 Å

40350

8sda

EMDB-40350, PDB-8sda:
CryoEM structure of rat Kv2.1(1-598) L403A mutant in nanodiscs
Method: EM (single particle) / Resolution: 3.32 Å

Chemicals

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM / POPC

ChemComp-K:
Unknown entry

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / voltage-dependent potassium channel

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