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TitleStructure of the human sodium leak channel NALCN in complex with FAM155A.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5831, Year 2020
Publish dateNov 17, 2020
AuthorsJiongfang Xie / Meng Ke / Lizhen Xu / Shiyi Lin / Jin Huang / Jiabei Zhang / Fan Yang / Jianping Wu / Zhen Yan /
PubMed AbstractNALCN, a sodium leak channel expressed mainly in the central nervous system, is responsible for the resting Na permeability that controls neuronal excitability. Dysfunctions of the NALCN ...NALCN, a sodium leak channel expressed mainly in the central nervous system, is responsible for the resting Na permeability that controls neuronal excitability. Dysfunctions of the NALCN channelosome, NALCN with several auxiliary subunits, are associated with a variety of human diseases. Here, we report the cryo-EM structure of human NALCN in complex with FAM155A at an overall resolution of 3.1 angstroms. FAM155A forms extensive interactions with the extracellular loops of NALCN that may help stabilize NALCN in the membrane. A Na ion-binding site, reminiscent of a Ca binding site in Ca channels, is identified in the unique EEKE selectivity filter. Despite its 'leaky' nature, the channel is closed and the intracellular gate is sealed by S6, II-III linker and III-IV linker. Our study establishes the molecular basis of Na permeation and voltage sensitivity, and provides important clues to the mechanistic understanding of NALCN regulation and NALCN channelosome-related diseases.
External linksNat Commun / PubMed:33203861 / PubMed Central
MethodsEM (single particle)
Resolution3.1 Å
Structure data

30400

7cm3

EMDB-30400, PDB-7cm3:
Cryo-EM structure of human NALCN in complex with FAM155A
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Ion channel

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