Component
SRC-2-derived HKILHRLL coactivator peptide
Synthetic eight-residue HKILHRLL peptide derived from SRC-2/NCOA2; not full-length coactivator.
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.
Where it participates (unsigned role)
T3 was bound within the human THRB ligand-binding domain in the crystallized THRB–RXRA domain heterodimer, with the THRB activation surface accommodating an SRC-2-derived peptide.
Experimental context and source evidence
- cross_nutrient
- An iodine-containing hormone binds THRB in a complex with the retinoid receptor RXRA; no nutritional vitamin A manipulation.
- evidence_locator
- Figure 2a and Results: structural characterization; Methods: protein production and crystallography
- evidence_spans
- [{"source_document": "artifacts/iodine-metabolism-sources/26289479.txt", "locator": "Figure 2a and Results: structural characterization; Methods: protein production and crystallography", "start_char": 10702, "end_char": 12152}]
- experimental_model
- Human TR beta/RXR alpha ligand-binding-domain crystallography; full-length human receptors in CV-1 reporter assays
- exposure
- Human THRB residues 202–461 and RXRA residues 223–462; threefold molar excess of T3 and synthetic HKILHRLL SRC-2 peptide; structure refined at anisotropic 3.2–3.8 angstrom resolution.
- limitations
- Isolated domains and an eight-residue peptide, not full-length coactivator recruitment in tissue. The structure establishes binding geometry, not a physiological T3 threshold.
- nutrient_topic
- Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
- organism
- Human receptor domains produced in Escherichia coli; synthetic coactivator peptide
- plain_language
- T3 physically occupies its receptor, which presents a docking surface for a transcription coactivator.
- primary_references
- [i-met-26289479] Structural mechanism for signal transduction in RXR nuclear receptor heterodimers. (2015). https://pubmed.ncbi.nlm.nih.gov/26289479/ DOI: 10.1038/ncomms9013
- tissue_or_cell_type
- Purified receptor-domain complex
Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 1172–1185
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human TR beta/RXR alpha ligand-binding-domain crystallography; full-length human receptors in CV-1 reporter assays · source_derived_draft · unverified_draft
### i-met-t3-thrb-ligand-binding T3 was bound within the human THRB ligand-binding domain in the crystallized THRB–RXRA domain heterodimer, with the THRB activation surface accommodating an SRC-2-derived peptide. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: T3 physically occupies its receptor, which presents a docking surface for a transcription coactivator. organism: Human receptor domains produced in Escherichia coli; synthetic coactivator peptide tissue_or_cell_type: Purified receptor-domain complex experimental_model: Human TR beta/RXR alpha ligand-binding-domain crystallography; full-length human receptors in CV-1 reporter assays limitations: Isolated domains and an eight-residue peptide, not full-length coactivator recruitment in tissue. The structure establishes binding geometry, not a physiological T3 threshold. exposure: Human THRB residues 202–461 and RXRA residues 223–462; threefold molar excess of T3 and synthetic HKILHRLL SRC-2 peptide; structure refined at anisotropic 3.2–3.8 angstrom resolution. cross_nutrient: An iodine-containing hormone binds THRB in a complex with the retinoid receptor RXRA; no nutritional vitamin A manipulation. evidence_locator: Figure 2a and Results: structural characterization; Methods: protein production and crystallography evidence_spans: [{"source_document": "artifacts/iodine-metabolism-sources/26289479.txt", "locator": "Figure 2a and Results: structural characterization; Methods: protein production and crystallography", "start_char": 10702, "end_char": 12152}] [i-met-26289479] Structural mechanism for signal transduction in RXR nuclear receptor heterodimers. (2015). https://pubmed.ncbi.nlm.nih.gov/26289479/ DOI: 10.1038/ncomms9013
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.