{"id":"b6b69f3d-e978-53bc-937f-cd35dccf902a","stable_key":"aaa7baba-8689-56ab-ba1e-b71542bcb8e9:iodine-trans-nis-bound-ions","predicate":"binds","statement":"The iodide-bound cryo-EM structure of engineered rat NIS contained density assigned to one iodide and two sodium ions in the substrate-binding cavity.","claim_class":"identity","status":"source_derived_draft","evidence_grade":"ungraded","direction":"neutral","is_public":true,"mechanism_event_id":"be157b61-48fe-533c-8778-203fcd4b2718","mechanism_event_label":"The NIS structure shows where iodide and its two sodium partners bind.","subject":{"id":"853ecec3-0ac5-54aa-891e-7afbd6b448b5","slug":"rat-slc5a5-unglycosylated-tagged","display_name":"Tagged rat NIS N225Q/N485Q/N497Q","entity_type_key":"protein_state"},"object":{"id":"83b11ca6-52c7-5a1b-8c39-d9cdf89244e3","slug":"iodide","display_name":"Iodide ion","entity_type_key":"ion"},"evidence_count":1,"mechanism_event":{"id":"be157b61-48fe-533c-8778-203fcd4b2718","stable_key":"aaa7baba-8689-56ab-ba1e-b71542bcb8e9:iodine-trans-nis-bound-ions-event","event_type":"biochemical_relationship","label":"The NIS structure shows where iodide and its two sodium partners bind.","description":"The iodide-bound cryo-EM structure of engineered rat NIS contained density assigned to one iodide and two sodium ions in the substrate-binding cavity.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"38de8704-84db-5770-ac1d-242cd787e798","slug":"sodium-ion","display_name":"Sodium ion","entity_type_key":"ion"},"role":"bound_cotransported_ion","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"83b11ca6-52c7-5a1b-8c39-d9cdf89244e3","slug":"iodide","display_name":"Iodide ion","entity_type_key":"ion"},"role":"bound_substrate","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"acfbc5ec-b299-5365-8c5d-9e492c18d1d9","slug":"rat-slc5a5","display_name":"Rat sodium/iodide symporter / Slc5a5","entity_type_key":"protein"},"role":"wild_type_reference","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"853ecec3-0ac5-54aa-891e-7afbd6b448b5","slug":"rat-slc5a5-unglycosylated-tagged","display_name":"Tagged rat NIS N225Q/N485Q/N497Q","entity_type_key":"protein_state"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"true","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Tagged N225Q/N485Q/N497Q rat NIS; iodide-bound structure at 3.12 Å.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Structural ion assignments and engineered construct support a binding mechanism; they do not alone measure physiological transport rates.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Iodine research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"iodine","display_name":"Iodine","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Rat protein produced in human 293F cells","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The NIS structure shows where iodide and its two sodium partners bind.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[iodine-trans-nis-structure2022] Structural insights into the mechanism of the sodium/iodide symporter. (2022). https://pubmed.ncbi.nlm.nih.gov/36517601/ DOI: 10.1038/s41586-022-05530-2","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified detergent-solubilized membrane protein","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"411bc3fa-3c21-55be-b226-e5919774e857","evidence_kind":"source_excerpt","locator":"Lines 193-204","start_line":193,"end_line":204,"excerpt":"### iodine-trans-nis-bound-ions\nThe iodide-bound cryo-EM structure of engineered rat NIS contained density assigned to one iodide and two sodium ions in the substrate-binding cavity.\nCondition category: normal\nnutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The NIS structure shows where iodide and its two sodium partners bind.\norganism: Rat protein produced in human 293F cells\ntissue_or_cell_type: Purified detergent-solubilized membrane protein\nexperimental_model: Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison\nlimitations: Structural ion assignments and engineered construct support a binding mechanism; they do not alone measure physiological transport rates.\nexposure: Tagged N225Q/N485Q/N497Q rat NIS; iodide-bound structure at 3.12 Å.\ncross_nutrient: true\n[iodine-trans-nis-structure2022] Structural insights into the mechanism of the sodium/iodide symporter. (2022). https://pubmed.ncbi.nlm.nih.gov/36517601/ DOI: 10.1038/s41586-022-05530-2","model_system":"Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [iodine-trans-nis-structure2022] Structural insights into the mechanism of the sodium/iodide symporter. (2022). https://pubmed.ncbi.nlm.nih.gov/36517601/ DOI: 10.1038/s41586-022-05530-2","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"76da623d-a34a-5a5c-a942-d7571a85c486","stable_key":"import-aaa7baba-8689-56ab-ba1e-b71542bcb8e9","title":"Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. 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