Component
Tagged rat NIS N225Q/N485Q/N497Q
Recombinant rat NIS with three glycosylation-site Asn-to-Gln substitutions and HA/HIS/SBP tags used for cryo-EM; reported activity comparable to wild type.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
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.
Experimental context and source evidence
- cross_nutrient
- true
- experimental_model
- Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison
- exposure
- Tagged N225Q/N485Q/N497Q rat NIS; iodide-bound structure at 3.12 Å.
- limitations
- Structural ion assignments and engineered construct support a binding mechanism; they do not alone measure physiological transport rates.
- nutrient_topic
- Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
- organism
- Rat protein produced in human 293F cells
- plain_language
- The NIS structure shows where iodide and its two sodium partners bind.
- primary_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
- tissue_or_cell_type
- Purified detergent-solubilized membrane protein
Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 193–204
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison · source_derived_draft · unverified_draft
### iodine-trans-nis-bound-ions 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. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The NIS structure shows where iodide and its two sodium partners bind. organism: Rat protein produced in human 293F cells tissue_or_cell_type: Purified detergent-solubilized membrane protein experimental_model: Purified tagged unglycosylated rat NIS expressed in human 293F cells; cryo-EM and functional comparison limitations: Structural ion assignments and engineered construct support a binding mechanism; they do not alone measure physiological transport rates. exposure: Tagged N225Q/N485Q/N497Q rat NIS; iodide-bound structure at 3.12 Å. cross_nutrient: true [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
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.