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Yorodumi- PDB-9y80: Homomeric Glycine Receptor alpha2 with PTX in a Desensitized State -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9y80 | |||||||||||||||||||||||||||
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| Title | Homomeric Glycine Receptor alpha2 with PTX in a Desensitized State | |||||||||||||||||||||||||||
Components | Glycine receptor subunit alpha-2 | |||||||||||||||||||||||||||
Keywords | TRANSPORT PROTEIN / homopentamer / ion channel / ligand gated ion channel | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationglycine-gated chloride ion channel activity / Neurotransmitter receptors and postsynaptic signal transmission / extracellularly glycine-gated chloride channel activity / glycinergic synapse / excitatory extracellular ligand-gated monoatomic ion channel activity / postsynaptic specialization membrane / glycine binding / cellular response to zinc ion / cellular response to ethanol / chloride channel complex ...glycine-gated chloride ion channel activity / Neurotransmitter receptors and postsynaptic signal transmission / extracellularly glycine-gated chloride channel activity / glycinergic synapse / excitatory extracellular ligand-gated monoatomic ion channel activity / postsynaptic specialization membrane / glycine binding / cellular response to zinc ion / cellular response to ethanol / chloride channel complex / cell projection / chloride transmembrane transport / cellular response to amino acid stimulus / neuropeptide signaling pathway / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / modulation of chemical synaptic transmission / GABA-ergic synapse / transmembrane signaling receptor activity / monoatomic ion transmembrane transport / metal ion binding / plasma membrane Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.55 Å | |||||||||||||||||||||||||||
Authors | Klemm, E. / Gibbs, E. / Chakrapani, S. | |||||||||||||||||||||||||||
| Funding support | United States, 3items
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Citation | Journal: Structure / Year: 2026Title: Human GlyRα2 pore dynamics in gating and inhibition. Authors: Emily Klemm / Eric Gibbs / Madeleine Stauffer / Devesh Mohapatra / Chloe Meyer / Sudha Chakrapani / ![]() Abstract: Glycine receptors (GlyRs) mediate inhibitory neurotransmission in the central nervous system. The GlyRα2 subtype contributes to critical neural circuitry in early neurodevelopment and is also found ...Glycine receptors (GlyRs) mediate inhibitory neurotransmission in the central nervous system. The GlyRα2 subtype contributes to critical neural circuitry in early neurodevelopment and is also found in adults. GlyRα2 dysfunctions are implicated in neurodevelopmental disorders, including autism, epilepsy, and cognitive delays. GlyRα2 functional properties and pharmacology are distinct from GlyRα1, but the structural basis for these differences remains poorly defined. Here, we report cryo-electron microscopy structures of full-length, human GlyRα2 reconstituted in peptidiscs captured in multiple conformational states. In addition to symmetric resting and desensitized states, we resolved an asymmetric open state, previously observed only in heteromeric GlyRs. This suggests that asymmetry is intrinsic to GlyRα2, independent of β-subunit incorporation. Furthermore, we identified distinct conformations of GlyRα2 with the pore-blocker picrotoxin, providing new insights into allosteric interactions. These findings uncover the structural basis of GlyRα2 function, providing a foundation for understanding its role in development and in GlyRα2-associated disorders. | |||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9y80.cif.gz | 328 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9y80.ent.gz | 264 KB | Display | PDB format |
| PDBx/mmJSON format | 9y80.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y8/9y80 ftp://data.pdbj.org/pub/pdb/validation_reports/y8/9y80 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72676MC ![]() 9y7pC ![]() 9y7wC ![]() 9y7xC ![]() 9y7zC ![]() 9y8zC ![]() 9y94C ![]() 9y95C ![]() 9y96C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 53782.840 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GLRA2Production host: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)References: UniProt: P23416 #2: Sugar | ChemComp-NAG / #3: Chemical | ChemComp-GLY / #4: Chemical | ChemComp-RI5 / ( | #5: Chemical | ChemComp-PX4 / Has ligand of interest | Y | Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Homomeric Glycine Receptor alpha2 with PTX in a Desensitized State Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths) |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| 3D reconstruction | Resolution: 3.55 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 100331 / Symmetry type: POINT |
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About Yorodumi



Homo sapiens (human)
United States, 3items
Citation
















PDBj






gel filtration
Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)




