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- EMDB-27555: Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer... -
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Open data
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Basic information
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Title | Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state1(open state) | |||||||||
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![]() | glycine receptor subunit alpha-1 / glycine receptor subunit beta / Green fluorescent protein / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() taurine binding / glycine-gated chloride channel complex / negative regulation of transmission of nerve impulse / Neurotransmitter receptors and postsynaptic signal transmission / acrosome reaction / positive regulation of acrosome reaction / gamma-aminobutyric acid receptor clustering / postsynaptic specialization / response to alcohol / neuromuscular process controlling posture ...taurine binding / glycine-gated chloride channel complex / negative regulation of transmission of nerve impulse / Neurotransmitter receptors and postsynaptic signal transmission / acrosome reaction / positive regulation of acrosome reaction / gamma-aminobutyric acid receptor clustering / postsynaptic specialization / response to alcohol / neuromuscular process controlling posture / inhibitory synapse / extracellularly glycine-gated ion channel activity / regulation of respiratory gaseous exchange by nervous system process / righting reflex / extracellularly glycine-gated chloride channel activity / synaptic transmission, glycinergic / glycinergic synapse / inhibitory postsynaptic potential / cellular response to ethanol / adult walking behavior / chloride transport / cellular response to zinc ion / neurotransmitter receptor activity / glycine binding / startle response / chloride channel complex / neuronal action potential / transmembrane transporter complex / GABA-ergic synapse / neuropeptide signaling pathway / monoatomic ion transport / muscle contraction / chloride transmembrane transport / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / visual perception / bioluminescence / regulation of membrane potential / generation of precursor metabolites and energy / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / cellular response to amino acid stimulus / transmembrane signaling receptor activity / nervous system development / chemical synaptic transmission / postsynaptic membrane / perikaryon / neuron projection / external side of plasma membrane / intracellular membrane-bounded organelle / neuronal cell body / synapse / dendrite / protein-containing complex binding / zinc ion binding / identical protein binding / membrane / plasma membrane / cytoplasm Similarity search - Function | |||||||||
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Method | single particle reconstruction / cryo EM / Resolution: 3.63 Å | |||||||||
![]() | Liu X / Wang W | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Asymmetric gating of a human hetero-pentameric glycine receptor. Authors: Xiaofen Liu / Weiwei Wang / ![]() Abstract: 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 ...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. | |||||||||
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 86 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.8 KB 20.8 KB | Display Display | ![]() |
Images | ![]() | 115.4 KB | ||
Filedesc metadata | ![]() | 7 KB | ||
Others | ![]() ![]() | 84.6 MB 84.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8dn5MC ![]() 8dn2C ![]() 8dn3C ![]() 8dn4C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
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Projections & Slices |
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
+Entire : heteromeric glycine receptor subunit alpha-1 and beta, glycine-bo...
+Supramolecule #1: heteromeric glycine receptor subunit alpha-1 and beta, glycine-bo...
+Macromolecule #1: Glycine receptor subunit alpha-1
+Macromolecule #2: Glycine receptor subunit beta,Green fluorescent protein,Glycine r...
+Macromolecule #3: GLYCINE
+Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose
+Macromolecule #5: nonane
+Macromolecule #6: HEPTANE
+Macromolecule #7: HEXANE
+Macromolecule #8: UNDECANE
+Macromolecule #9: N-BUTANE
+Macromolecule #10: DECANE
+Macromolecule #11: N-OCTANE
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 6 mg/mL | ||||||||||||
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Buffer | pH: 8 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 70 sec. | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 69.6 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: GATAN LIQUID NITROGEN / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.63 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 21676 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |