{
  "abstract": "The gating and function of γ-aminobutyric acid type A receptors (GABAARs) depend on their hetero-pentameric subunit composition, yet the rules guiding subunit selection remain unclear. We show that a conserved N-linked glycan in α subunits, uniquely positioned within the extracellular pore, acts as a structural constraint that limits the functional viability of α-containing assemblies. A total of 32 µs of molecular dynamics simulations of native and hypothetical non-canonical assemblies show that adding a third pore-facing glycan or placing two glycans on adjacent subunits disrupts key interactions at the β+/α– interface containing the GABA-binding site. These perturbations propagate allosterically, alter extracellular–transmembrane domain coupling, and promote deep gate closure. Systems with three pore-facing glycans consistently adopt deep-closed conformations, whereas native assemblies with two glycans preserve interfacial integrity and pore hydration. These results identify the pore-facing glycan as a structural constraint on functionally viable GABAAR architecture and gating.",
  "abstract_shown": true,
  "affiliations": [
    "Department of BioMolecular Sciences, School of Pharmacy, University of Mississippi"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Amin Akbari-Ahangar"
    },
    {
      "affs": [
        0
      ],
      "name": "Jing Li"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/dq3vedks2dhe6.bib",
  "cited_by": 0,
  "doi": "10.1038/s42003-026-10547-8",
  "fulltext_url": "https://doi.org/10.1038/s42003-026-10547-8",
  "id": "dq3vedks2dhe6",
  "issns": [
    "2399-3642"
  ],
  "landing_url": "https://doi.org/10.1038/s42003-026-10547-8",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "lcc",
      "QH301-705.5"
    ],
    [
      "openalex",
      "2804|Neuroscience and Neuropharmacology Research"
    ]
  ],
  "openalex": "W7167032788",
  "pdf_url": null,
  "pmcid": null,
  "pmid": null,
  "published": "2026-07-01",
  "publisher": "Nature Portfolio",
  "ris": "https://research.draconitic.com/paper/dq3vedks2dhe6.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T13:46:20Z",
      "native_id": "489321fbb65c4b52bfd68a2919500272",
      "source": "doaj",
      "url": "https://doi.org/10.1038/s42003-026-10547-8"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "openalex:2804|Neuroscience and Neuropharmacology Research",
      "subfield": "neuroscience"
    }
  ],
  "title": "A pore-facing glycan constrains GABAA receptor subunit stoichiometry and gating behavior",
  "title_text": "A pore-facing glycan constrains GABAA receptor subunit stoichiometry and gating behavior",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T13:46:20Z",
  "url": "https://research.draconitic.com/paper/dq3vedks2dhe6",
  "venue": "Communications Biology",
  "versions": []
}