{"id":"a84b86bf-9682-5438-bd11-adcf0a13ab3e","stable_key":"195e8b84-ca5a-591a-a045-c55c53c8a01c:sodium-nav14-pore","predicate":"forms_selective_pore_for","statement":"The human Nav1.4–beta1 structure resolved its pore and voltage-sensing domains, supporting a molecular account of sodium permeation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"31137d41-dfc8-5bd2-8a18-3d337fe9083d","mechanism_event_label":"A dedicated sodium-channel protein helps electrically excitable cells generate signals.","subject":{"id":"983f1cd8-6683-5f0c-8bd9-1d1959de5402","slug":"scn4a","display_name":"NaV1.4 / SCN4A","entity_type_key":"protein"},"object":{"id":"38de8704-84db-5770-ac1d-242cd787e798","slug":"sodium-ion","display_name":"Sodium ion","entity_type_key":"ion"},"evidence_count":1,"mechanism_event":{"id":"31137d41-dfc8-5bd2-8a18-3d337fe9083d","stable_key":"195e8b84-ca5a-591a-a045-c55c53c8a01c:sodium-nav14-pore-event","event_type":"biochemical_relationship","label":"A dedicated sodium-channel protein helps electrically excitable cells generate signals.","description":"The human Nav1.4–beta1 structure resolved its pore and voltage-sensing domains, supporting a molecular account of sodium permeation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"19fe92f8-b0a9-53ed-9818-43f2c827836c","slug":"scn1b","display_name":"Human sodium-channel beta1 subunit / SCN1B","entity_type_key":"protein"},"role":"auxiliary_subunit","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"983f1cd8-6683-5f0c-8bd9-1d1959de5402","slug":"scn4a","display_name":"NaV1.4 / SCN4A","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"38de8704-84db-5770-ac1d-242cd787e798","slug":"sodium-ion","display_name":"Sodium ion","entity_type_key":"ion"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/sodium-research/30190309.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436\", \"start_char\": 0, \"end_char\": 876, \"text_sha256\": \"2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Cryo-EM reconstruction at 3.2 angstrom resolution","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Purified Nav1.4–beta1 structure","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Structural support for permeation and inactivation; this experiment did not test dietary sodium or clinical supplementation.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Sodium research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"sodium","display_name":"Sodium","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Human channel complex","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A dedicated sodium-channel protein helps electrically excitable cells generate signals.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[sodium-p30190309] Structure of the human voltage-gated sodium channel Nav1.4 in complex with β1. (2018). https://pubmed.ncbi.nlm.nih.gov/30190309/ DOI: 10.1126/science.aau2486","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Skeletal-muscle Nav1.4 with beta1","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"7bf90906-eeef-5914-a08c-c4467b18e205","evidence_kind":"source_excerpt","locator":"Lines 343-354","start_line":343,"end_line":354,"excerpt":"### sodium-nav14-pore\nThe human Nav1.4–beta1 structure resolved its pore and voltage-sensing domains, supporting a molecular account of sodium permeation.\nCondition category: normal\nnutrient_topic: Sodium research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A dedicated sodium-channel protein helps electrically excitable cells generate signals.\norganism: Human channel complex\ntissue_or_cell_type: Skeletal-muscle Nav1.4 with beta1\nexperimental_model: Cryo-EM reconstruction at 3.2 angstrom resolution\nlimitations: Structural support for permeation and inactivation; this experiment did not test dietary sodium or clinical supplementation.\nexposure: Purified Nav1.4–beta1 structure\nevidence_span: {\"source_cache\": \"artifacts/sodium-research/30190309.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436\", \"start_char\": 0, \"end_char\": 876, \"text_sha256\": \"2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436\"}\n[sodium-p30190309] Structure of the human voltage-gated sodium channel Nav1.4 in complex with β1. (2018). https://pubmed.ncbi.nlm.nih.gov/30190309/ DOI: 10.1126/science.aau2486","model_system":"Cryo-EM reconstruction at 3.2 angstrom resolution","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [sodium-p30190309] Structure of the human voltage-gated sodium channel Nav1.4 in complex with β1. (2018). https://pubmed.ncbi.nlm.nih.gov/30190309/ DOI: 10.1126/science.aau2486","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"c260cd7b-beb0-5113-a198-69ec8fd4492c","stable_key":"import-195e8b84-ca5a-591a-a045-c55c53c8a01c","title":"Sodium: gradients, nutrient transport, fluid regulation and loss states (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"684f65cf0661c18395831ade4b02bb24d5e66c568f0d00a3471600eaf5d4d1c6","revision_id":"39866f04-3052-5f59-bd95-6806c5490875","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}