{
  "annotation_id": "35d3343d-ab30-4604-bd4a-0620b3cb2404",
  "date_created": "2026-03-02T18:00:46.688000Z",
  "date_modified": "2026-03-02T18:00:46.688000Z",
  "file_hash": "52c212ea6bda325b50cb1695b6143fc7481de1458aeb3aa41fee37118ed1105f",
  "private": false,
  "record": {
    "abstract": "ClC chloride channels possess a homodimeric structure in which each monomer\ncontains an independent chloride ion pathway. ClC channel gating is regulated\nby chloride ion concentration, pH, and voltage. Based on structural and\nphysiological evidence, it has been proposed that a glutamate residue on the\nextracellular end of the selectivity filter acts as a fast gate. We utilize a\nnew search algorithm which incorporates electrostatic information to explore\nthe ion transit pathways through wild-type and mutant bacterial ClC channels.\nExamination of the chloride ion permeation pathways supports the proposed\nimportant role of the glutamate residue in gating. An external chloride binding\nsite previously postulated in physiological experiments is located near a\nconserved basic residue adjacent to the gate. In addition, access pathways are\nfound for proton migration to the gate, enabling pH control at hyperpolarized\nmembrane potentials. A chloride ion in the selectivity filter is required for\nthe pH-dependent gating mechanism.",
    "arxiv_id": "physics/0401022",
    "authors": [
      "J. Yin",
      "Z. Kuang",
      "U. Mahankali",
      "T. L. Beck"
    ],
    "categories": [
      "physics.bio-ph",
      "physics.chem-ph"
    ],
    "title": "Ion Transit Pathways and Gating in ClC Chloride Channels",
    "url": "https://arxiv.org/abs/physics/0401022"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "761b561f-3ff2-49c3-9f61-54dccc425f89",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}