Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex
The NALCN channel mediates sodium leak currents, which in turn adjusts resting membrane potential and neuronal excitability. Here the authors describe a cryo-EM structure of mammalian NALCN-FAM155A channel complex, showing how selectivity filter contributes to sodium permeation and calcium block and...
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2020-12-01
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Online Access: | https://doi.org/10.1038/s41467-020-20002-9 |
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doaj-4a01fb3b9eac4a6eaaf11895ad50315c2021-05-11T08:47:51ZengNature Publishing GroupNature Communications2041-17232020-12-0111111010.1038/s41467-020-20002-9Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complexYunlu Kang0Jing-Xiang Wu1Lei Chen2State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking UniversityState Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking UniversityState Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking UniversityThe NALCN channel mediates sodium leak currents, which in turn adjusts resting membrane potential and neuronal excitability. Here the authors describe a cryo-EM structure of mammalian NALCN-FAM155A channel complex, showing how selectivity filter contributes to sodium permeation and calcium block and how the voltage sensors contribute to current modulation.https://doi.org/10.1038/s41467-020-20002-9 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yunlu Kang Jing-Xiang Wu Lei Chen |
spellingShingle |
Yunlu Kang Jing-Xiang Wu Lei Chen Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex Nature Communications |
author_facet |
Yunlu Kang Jing-Xiang Wu Lei Chen |
author_sort |
Yunlu Kang |
title |
Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex |
title_short |
Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex |
title_full |
Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex |
title_fullStr |
Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex |
title_full_unstemmed |
Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex |
title_sort |
structure of voltage-modulated sodium-selective nalcn-fam155a channel complex |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2020-12-01 |
description |
The NALCN channel mediates sodium leak currents, which in turn adjusts resting membrane potential and neuronal excitability. Here the authors describe a cryo-EM structure of mammalian NALCN-FAM155A channel complex, showing how selectivity filter contributes to sodium permeation and calcium block and how the voltage sensors contribute to current modulation. |
url |
https://doi.org/10.1038/s41467-020-20002-9 |
work_keys_str_mv |
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1721450420142866432 |