{"id":"58a78ce4-74b2-5ca0-8d97-cb35d720ca4c","stable_key":"195e8b84-ca5a-591a-a045-c55c53c8a01c:sodium-nav14-inactivation","predicate":"structurally_supports","statement":"Analysis of the Nav1.4 structure and previously characterized residues supported an allosteric blocking mechanism of fast inactivation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"29ecd015-5034-51c3-9a10-51b7dc3241b2","mechanism_event_label":"The channel has a mechanism to stop sodium flow rapidly after activation.","subject":{"id":"983f1cd8-6683-5f0c-8bd9-1d1959de5402","slug":"scn4a","display_name":"NaV1.4 / SCN4A","entity_type_key":"protein"},"object":{"id":"bc94e348-e65d-5a24-87cc-5b601806728a","slug":"nav14-fast-inactivation","display_name":"Nav1.4 fast inactivation","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"29ecd015-5034-51c3-9a10-51b7dc3241b2","stable_key":"195e8b84-ca5a-591a-a045-c55c53c8a01c:sodium-nav14-inactivation-event","event_type":"biochemical_relationship","label":"The channel has a mechanism to stop sodium flow rapidly after activation.","description":"Analysis of the Nav1.4 structure and previously characterized residues supported an allosteric blocking mechanism of fast inactivation.","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":"bc94e348-e65d-5a24-87cc-5b601806728a","slug":"nav14-fast-inactivation","display_name":"Nav1.4 fast inactivation","entity_type_key":"cellular_process"},"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":"The channel has a mechanism to stop sodium flow rapidly after activation.","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":"6e33879e-5bc2-528d-afa2-b29046cdd993","evidence_kind":"source_excerpt","locator":"Lines 356-367","start_line":356,"end_line":367,"excerpt":"### sodium-nav14-inactivation\nAnalysis of the Nav1.4 structure and previously characterized residues supported an allosteric blocking mechanism of fast inactivation.\nCondition category: normal\nnutrient_topic: Sodium research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The channel has a mechanism to stop sodium flow rapidly after activation.\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. 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