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TitleStructural principles of distinct assemblies of the human α4β2 nicotinic receptor.
Journal, issue, pagesNature, Vol. 557, Issue 7704, Page 261-265, Year 2018
Publish dateMay 2, 2018
AuthorsRichard M Walsh / Soung-Hun Roh / Anant Gharpure / Claudio L Morales-Perez / Jinfeng Teng / Ryan E Hibbs /
PubMed AbstractFast chemical communication in the nervous system is mediated by neurotransmitter-gated ion channels. The prototypical member of this class of cell surface receptors is the cation-selective nicotinic ...Fast chemical communication in the nervous system is mediated by neurotransmitter-gated ion channels. The prototypical member of this class of cell surface receptors is the cation-selective nicotinic acetylcholine receptor. As with most ligand-gated ion channels, nicotinic receptors assemble as oligomers of subunits, usually as hetero-oligomers and often with variable stoichiometries . This intrinsic heterogeneity in protein composition provides fine tunability in channel properties, which is essential to brain function, but frustrates structural and biophysical characterization. The α4β2 subtype of the nicotinic acetylcholine receptor is the most abundant isoform in the human brain and is the principal target in nicotine addiction. This pentameric ligand-gated ion channel assembles in two stoichiometries of α- and β-subunits (2α:3β and 3α:2β). Both assemblies are functional and have distinct biophysical properties, and an imbalance in the ratio of assemblies is linked to both nicotine addiction and congenital epilepsy. Here we leverage cryo-electron microscopy to obtain structures of both receptor assemblies from a single sample. Antibody fragments specific to β2 were used to 'break' symmetry during particle alignment and to obtain high-resolution reconstructions of receptors of both stoichiometries in complex with nicotine. The results reveal principles of subunit assembly and the structural basis of the distinctive biophysical and pharmacological properties of the two different stoichiometries of this receptor.
External linksNature / PubMed:29720657 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 3.9 Å
Structure data

7535

6cnj

EMDB-7535, PDB-6cnj:
Structure of the 2alpha3beta stiochiometry of the human Alpha4Beta2 nicotinic receptor
Method: EM (single particle) / Resolution: 3.7 Å

7536

6cnk

EMDB-7536, PDB-6cnk:
Structure of the 3alpha2beta stiochiometry of the human Alpha4Beta2 nicotinic receptor
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-NCT:
(S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE / alkaloid*YM / Nicotine

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
  • house mouse (house mouse)
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / Ligand-gated ion channel / Acetylcholine receptor / Cys-loop Receptor / MEMBRANE PROTEIN

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