Component
FKBP-FK506 complex
The second immunophilin-drug complex that inhibits calcineurin, structurally unrelated to the cyclophilin one.
2 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 FKBP-FK506 complex also competitively binds and inhibits calcineurin, making calcineurin the common target of two structurally unrelated immunophilin-drug complexes.
Experimental context and source evidence
- duration
- Not stated here
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Purified mammalian proteins
- exposure
- FKBP complexed with FK506 (tacrolimus)
- limitations
- Convergence on one target does not make the two drugs interchangeable; their immunophilins, their tissue distribution and their other complexes differ, and none of that is measured here.
- organism
- Purified mammalian proteins
- plain_language
- The FKBP-FK506 complex also competitively binds and inhibits calcineurin, making calcineurin the common target of two structurally unrelated immunophilin-drug complexes.
- primary_references
- Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. (1991). https://pubmed.ncbi.nlm.nih.gov/1715244/ DOI: 10.1016/0092-8674(91)90124-h
- route
- In vitro
- tissue
- Calcineurin phosphatase activity
Original AI-assisted curation of seven primary studies resolved by PubMed title search, with every abstract read and all DOIs cross-checked against live PubMed metadata on 2026-09-23. No reference carries a recorded retraction, erratum or expression of concern. Each of the seven is a separate laboratory and each carries its own lineage key, so none of them can be counted twice as independent support. Study-specific concentrations, kinetic constants and limitations retained. Not publisher full text. · supports · Purified mammalian proteins · source_derived_draft · unverified_draft
The FKBP-FK506 complex also competitively binds and inhibits calcineurin, making calcineurin the common target of two structurally unrelated immunophilin-drug complexes.
Complete structured claim and evidence
What acts on it
FK506 likewise acts by forming a drug-dependent complex with FKBP, and it is that complex, not the free drug, that binds and inhibits calcineurin.
Experimental context and source evidence
- duration
- Not stated here
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Purified mammalian proteins
- exposure
- FK506 (tacrolimus) with FKBP
- limitations
- Recorded so that the tacrolimus side of this convergence is drawn the same way as the cyclosporine side. The report does not measure the rate or affinity of complex formation itself.
- organism
- Purified mammalian proteins
- plain_language
- FK506 likewise acts by forming a drug-dependent complex with FKBP, and it is that complex, not the free drug, that binds and inhibits calcineurin.
- primary_references
- Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. (1991). https://pubmed.ncbi.nlm.nih.gov/1715244/ DOI: 10.1016/0092-8674(91)90124-h
- route
- In vitro
- tissue
- Formation of the drug-immunophilin complex
Original AI-assisted curation of seven primary studies resolved by PubMed title search, with every abstract read and all DOIs cross-checked against live PubMed metadata on 2026-09-23. No reference carries a recorded retraction, erratum or expression of concern. Each of the seven is a separate laboratory and each carries its own lineage key, so none of them can be counted twice as independent support. Study-specific concentrations, kinetic constants and limitations retained. Not publisher full text. · supports · Purified mammalian proteins · source_derived_draft · unverified_draft
FK506 likewise acts by forming a drug-dependent complex with FKBP, and it is that complex, not the free drug, that binds and inhibits calcineurin.
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.