Component

Cyclophilin A-cyclosporine complex

The drug-immunophilin complex that inhibits calcineurin. Neither the drug alone nor the immunophilin alone does, which is why this is its own entity.

3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What it acts on

  1. In the 2.8-angstrom crystal structure the cyclophilin A-cyclosporin A complex binds a composite surface formed by the catalytic and regulatory subunits of calcineurin, and unlike FKBP-FK506 it also interacts with Arg-122 at the calcineurin active site.

    Cyclophilin A-cyclosporine complex → Calcineurin source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not applicable
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Recombinant human proteins in crystal
    exposure
    Cyclophilin A with cyclosporin A bound
    limitations
    A structure shows contact, not rate. The authors read the active-site contact as implying direct involvement in regulating catalysis, which is an interpretation and is recorded as one. No direction is recorded for this claim, because a binding geometry is not itself an increase or a decrease.
    organism
    Recombinant human proteins in crystal
    plain_language
    In the 2.8-angstrom crystal structure the cyclophilin A-cyclosporin A complex binds a composite surface formed by the catalytic and regulatory subunits of calcineurin, and unlike FKBP-FK506 it also interacts with Arg-122 at the calcineurin active site.
    primary_references
    Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. (2002). https://pubmed.ncbi.nlm.nih.gov/12218175/ DOI: 10.1073/pnas.192206699
    route
    In vitro
    tissue
    Calcineurin catalytic and regulatory subunit interface

    Cyclosporine: the complex that inhibits calcineurin, a second cyclophilin, and the transport step that decides exposure (2026-09-23) · lines 91–91

    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 · Recombinant human proteins in crystal · source_derived_draft · unverified_draft

    In the 2.8-angstrom crystal structure the cyclophilin A-cyclosporin A complex binds a composite surface formed by the catalytic and regulatory subunits of calcineurin, and unlike FKBP-FK506 it also interacts with Arg-122 at the calcineurin active site.
    Complete structured claim and evidence

  2. The cyclophilin-cyclosporin A complex competitively binds and inhibits the calcium- and calmodulin-dependent phosphatase calcineurin.

    Cyclophilin A-cyclosporine complex → Calcineurin source_derived_draftungraded
    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
    Cyclophilin complexed with cyclosporin A
    limitations
    Binding and inhibition of calcineurin did not require calmodulin in this report. The inhibitor is the complex, not the drug, so this arrow must not be redrawn from cyclosporine directly to calcineurin.
    organism
    Purified mammalian proteins
    plain_language
    The cyclophilin-cyclosporin A complex competitively binds and inhibits the calcium- and calmodulin-dependent phosphatase 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
    Calcineurin phosphatase activity

    Cyclosporine: the complex that inhibits calcineurin, a second cyclophilin, and the transport step that decides exposure (2026-09-23) · lines 47–47

    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 cyclophilin-cyclosporin A complex competitively binds and inhibits the calcium- and calmodulin-dependent phosphatase calcineurin.
    Complete structured claim and evidence

What acts on it

  1. The effects of cyclosporin A are reported to follow from the formation of an inhibitory complex between the drug and its prolyl isomerase, and not from inhibition of the isomerase activity that drug binding also causes.

    Cyclosporine → Cyclophilin A-cyclosporine complex source_derived_draftungraded
    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
    Mammalian immunophilin biochemistry, with cyclosporin-resistant yeast mutants cited as support
    exposure
    Cyclosporin A with cyclophilin
    limitations
    This is the step that makes the drug an inhibitor of anything, and it is why no arrow in this collection runs from cyclosporine to calcineurin directly. The evidence cited for it in this report is the behaviour of other isomerase inhibitors and of cyclosporin-resistant yeast mutants, which is an argument from the pattern of results rather than a measurement of complex formation.
    organism
    Mammalian immunophilin biochemistry, with cyclosporin-resistant yeast mutants cited as support
    plain_language
    The effects of cyclosporin A are reported to follow from the formation of an inhibitory complex between the drug and its prolyl isomerase, and not from inhibition of the isomerase activity that drug binding also causes.
    primary_references
    Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A. (1991). https://pubmed.ncbi.nlm.nih.gov/1715516/ DOI: 10.1038/352803a0
    route
    In vitro
    tissue
    Formation of the drug-immunophilin complex

    Cyclosporine: the complex that inhibits calcineurin, a second cyclophilin, and the transport step that decides exposure (2026-09-23) · lines 25–25

    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 · Mammalian immunophilin biochemistry, with cyclosporin-resistant yeast mutants cited as support · source_derived_draft · unverified_draft

    The effects of cyclosporin A are reported to follow from the formation of an inhibitory complex between the drug and its prolyl isomerase, and not from inhibition of the isomerase activity that drug binding also causes.
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards