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Structure paper

TitleAsymmetric gating of a human hetero-pentameric glycine receptor.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 6377, Year 2023
Publish dateOct 11, 2023
AuthorsXiaofen Liu / Weiwei Wang /
PubMed AbstractHetero-pentameric Cys-loop receptors constitute a major type of neurotransmitter receptors that enable signal transmission and processing in the nervous system. Despite intense investigations into ...Hetero-pentameric Cys-loop receptors constitute a major type of neurotransmitter receptors that enable signal transmission and processing in the nervous system. Despite intense investigations into their working mechanism and pharmaceutical potentials, how neurotransmitters activate these receptors remains unclear due to the lack of high-resolution structural information in the activated open state. Here we report near-atomic resolution structures resolved in digitonin consistent with all principle functional states of the human α1β GlyR, which is a major Cys-loop receptor that mediates inhibitory neurotransmission in the central nervous system of adults. Glycine binding induces cooperative and symmetric structural rearrangements in the neurotransmitter-binding extracellular domain but asymmetrical pore dilation in the transmembrane domain. Symmetric response in the extracellular domain is consistent with electrophysiological data showing cooperative glycine activation and contribution from both α1 and β subunits. A set of functionally essential but differentially charged amino acid residues in the transmembrane domain of the α1 and β subunits explains asymmetric activation. These findings provide a foundation for understanding how the gating of the Cys-loop receptor family members diverges to accommodate specific physiological environments.
External linksNat Commun / PubMed:37821459 / PubMed Central
MethodsEM (single particle)
Resolution3.55 - 4.1 Å
Structure data

27552

8dn2

EMDB-27552, PDB-8dn2:
Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state 2(expanded open)
Method: EM (single particle) / Resolution: 3.9 Å

27553

8dn3

EMDB-27553, PDB-8dn3:
Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, apo state
Method: EM (single particle) / Resolution: 3.55 Å

27554

8dn4

EMDB-27554, PDB-8dn4:
Cryo-EM structure of human Glycine Receptor alpha-1 beta heteromer, glycine-bound state3(desensitized state)
Method: EM (single particle) / Resolution: 4.1 Å

27555

8dn5

EMDB-27555, PDB-8dn5:
Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state1(open state)
Method: EM (single particle) / Resolution: 3.63 Å

Chemicals

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

ChemComp-HEX:
HEXANE / Hexane

ChemComp-HP6:
HEPTANE / Heptane

ChemComp-UND:
UNDECANE / Undecane

ChemComp-OCT:
N-OCTANE / Octane

ChemComp-GLY:
GLYCINE / Glycine

ChemComp-DD9:
nonane / Nonane

ChemComp-NBU:
N-BUTANE / Butane

ChemComp-D10:
DECANE / Decane

ChemComp-CL:
Unknown entry / Chloride

ChemComp-LNK:
PENTANE / Pentane

Source
  • homo sapiens (human)
  • aequorea victoria (jellyfish)
KeywordsMEMBRANE PROTEIN / glycine receptor subunit alpha-1 / glycine receptor subunit beta / Green fluorescent protein

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