Component
Mouse alpha-tocopherol transfer protein
Mus musculus alpha-TTP; protein in the deposited Kono 2013 PDB 3W68 structure.
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 deposited mouse alpha-TTP complex contains alpha-tocopherol and PI(4,5)P2, with phosphoinositide binding at the protein surface linked to opening of its ligand pocket.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- X-ray complex PDB 3W68
- exposure
- Crystallized protein with alpha-tocopherol and PI(4,5)P2.
- limitations
- Structure is mouse protein; no dietary phosphorus requirement or human affinity value is inferred.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Mus musculus protein
- plain_language
- A membrane phosphoinositide interacts with the vitamin E transfer protein.
- primary_references
- [kono2013] Impaired α-TTP-PIPs interaction underlies familial vitamin E deficiency. (2013). https://pubmed.ncbi.nlm.nih.gov/23599266/ DOI: 10.1126/science.1233508
- tissue_or_cell_type
- Purified protein-lipid complex
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 324–335
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray complex PDB 3W68 · source_derived_draft · unverified_draft
### ve-transport-mouse-ttp-pip2-binding The deposited mouse alpha-TTP complex contains alpha-tocopherol and PI(4,5)P2, with phosphoinositide binding at the protein surface linked to opening of its ligand pocket. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: A membrane phosphoinositide interacts with the vitamin E transfer protein. organism: Mus musculus protein tissue_or_cell_type: Purified protein-lipid complex experimental_model: X-ray complex PDB 3W68 limitations: Structure is mouse protein; no dietary phosphorus requirement or human affinity value is inferred. exposure: Crystallized protein with alpha-tocopherol and PI(4,5)P2. cross_nutrient: false [kono2013] Impaired α-TTP-PIPs interaction underlies familial vitamin E deficiency. (2013). https://pubmed.ncbi.nlm.nih.gov/23599266/ DOI: 10.1126/science.1233508
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.