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Structure paper

TitleHuman GlyRα2 pore dynamics in gating and inhibition.
Journal, issue, pagesStructure, Year 2026
Publish dateMar 18, 2026
AuthorsEmily Klemm / Eric Gibbs / Madeleine Stauffer / Devesh Mohapatra / Chloe Meyer / Sudha Chakrapani /
PubMed AbstractGlycine 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.
External linksStructure / PubMed:41856109 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 3.6 Å
Structure data

72665

9y7p

EMDB-72665, PDB-9y7p:
Homomeric Glycine Receptor alpha2 with 1 mM Glycine in a Desensitized State
Method: EM (single particle) / Resolution: 2.5 Å

72668

9y7w

EMDB-72668, PDB-9y7w:
Homomeric Glycine Receptor alpha2 with 1 mM Glycine in an Open State
Method: EM (single particle) / Resolution: 3.19 Å

72674

9y7x

EMDB-72674, PDB-9y7x:
Homomeric Glycine Receptor alpha2 with 0.1 mM Glycine in an Open State
Method: EM (single particle) / Resolution: 3.55 Å

72675

9y7z

EMDB-72675, PDB-9y7z:
Homomeric Glycine Receptor alpha2 with 0.1 mM Glycine in a Desensitized State
Method: EM (single particle) / Resolution: 2.78 Å

72676

9y80

EMDB-72676, PDB-9y80:
Homomeric Glycine Receptor alpha2 with PTX in a Desensitized State
Method: EM (single particle) / Resolution: 3.55 Å

72683

9y8z

EMDB-72683, PDB-9y8z:
Homomeric Glycine Receptor alpha2 with 0.1 mM Glycine in an Apo State
Method: EM (single particle) / Resolution: 2.5 Å

72688

9y94

EMDB-72688, PDB-9y94:
Homomeric Glycine Receptor alpha2 with PTX in an Open State
Method: EM (single particle) / Resolution: 3.6 Å

72689

9y95

EMDB-72689, PDB-9y95:
Homomeric Glycine Receptor alpha2 with PTX in an Apo State
Method: EM (single particle) / Resolution: 3.45 Å

72690

9y96

EMDB-72690, PDB-9y96:
Homomeric Glycine Receptor alpha2 with 1 mM Glycine in a Closed State
Method: EM (single particle) / Resolution: 3.36 Å

Chemicals

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

ChemComp-GLY:
GLYCINE

ChemComp-PX4:
1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DMPC, phospholipid*YM

ChemComp-RI5:
(1aR,2aR,3S,6R,6aS,8aS,8bR,9R)-2a-hydroxy-8b-methyl-9-(prop-1-en-2-yl)hexahydro-3,6-methano-1,5,7-trioxacyclopenta[ij]c / toxin*YM

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / homopentamer / ion channel / ligand gated ion channel

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