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TitleStructural basis for excitatory neuropeptide signaling.
Journal, issue, pagesNat Struct Mol Biol, Vol. 31, Issue 4, Page 717-726, Year 2024
Publish dateFeb 9, 2024
AuthorsValeria Kalienkova / Mowgli Dandamudi / Cristina Paulino / Timothy Lynagh /
PubMed AbstractRapid signaling between neurons is mediated by ligand-gated ion channels, cell-surface proteins with an extracellular ligand-binding domain and a membrane-spanning ion channel domain. The ...Rapid signaling between neurons is mediated by ligand-gated ion channels, cell-surface proteins with an extracellular ligand-binding domain and a membrane-spanning ion channel domain. The degenerin/epithelial sodium channel (DEG/ENaC) superfamily is diverse in terms of its gating stimuli, with some DEG/ENaCs gated by neuropeptides, and others gated by pH, mechanical force or enzymatic activity. The mechanism by which ligands bind to and activate DEG/ENaCs is poorly understood. Here we dissected the structural basis for neuropeptide-gated activity of a neuropeptide-gated DEG/ENaC, FMRFamide-gated sodium channel 1 (FaNaC1) from the annelid worm Malacoceros fuliginosus, using cryo-electron microscopy. Structures of FaNaC1 in the ligand-free resting state and in several ligand-bound states reveal the ligand-binding site and capture the ligand-induced conformational changes of channel gating, which we verified with complementary mutagenesis experiments. Our results illuminate channel gating in DEG/ENaCs and offer a structural template for experimental dissection of channel pharmacology and ion conduction.
External linksNat Struct Mol Biol / PubMed:38337033 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 3.0 Å
Structure data

16981

8on7

EMDB-16981, PDB-8on7:
FMRFa-bound Malacoceros FaNaC1 in lipid nanodiscs
Method: EM (single particle) / Resolution: 2.5 Å

16982

8on8

EMDB-16982, PDB-8on8:
Apo Malacoceros FaNaC1 in lipid nanodiscs
Method: EM (single particle) / Resolution: 2.7 Å

16983

8on9

EMDB-16983, PDB-8on9:
ASSFVRIa-bound Malacoceros FaNaC1 in lipid nanodiscs
Method: EM (single particle) / Resolution: 2.4 Å

16984

8ona

EMDB-16984, PDB-8ona:
FMRFa-bound Malacoceros FaNaC1 in lipid nanodiscs in presence of diminazene
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

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

Source
  • malacoceros fuliginosus (invertebrata)
KeywordsMEMBRANE PROTEIN / Neuropeptide / ion channel / DEG/ENaC

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