Component
Human OCTN2 allosteric sodium-binding site
Context-specific entity; species, compartment and exposure are stated on each claim.
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 acts on it
Human OCTN2 cryo-EM structures identified a sodium-binding cavity separate from the carnitine site, with allosteric coupling supported by electrophysiology.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human OCTN2 structures in ligand-free, carnitine/sodium-bound and ipratropium-bound conformations; 2025 primary study.
- limitations
- Structural coupling does not show that more sodium intake increases transport.
- nutrient_topic
- L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
- plain_language
- Sodium supports transport through a separate coupled binding site.
- primary_references
- Structural basis of sodium ion-dependent carnitine transport by OCTN2. · 2025 · https://pubmed.ncbi.nlm.nih.gov/41318751/ · DOI 10.1038/s41467-025-66867-6
L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 490–496
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human OCTN2 structures in ligand-free, carnitine/sodium-bound and ipratropium-bound conformations; 2025 primary study. · source_derived_draft · unverified_draft
## l-carnitine-octn2-structure Sodium supports transport through a separate coupled binding site. Human OCTN2 cryo-EM structures identified a sodium-binding cavity separate from the carnitine site, with allosteric coupling supported by electrophysiology. Model: Human OCTN2 structures in ligand-free, carnitine/sodium-bound and ipratropium-bound conformations; 2025 primary study. Limitations: Structural coupling does not show that more sodium intake increases transport. Evidence access: Primary abstract Structural basis of sodium ion-dependent carnitine transport by OCTN2. · 2025 · https://pubmed.ncbi.nlm.nih.gov/41318751/ · DOI 10.1038/s41467-025-66867-6
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.