{"id":"f3f7534e-87f7-5243-805f-4a3b9ec2e9c0","stable_key":"1bbf9d44-8d2b-5b35-8f82-f6876558b0b3:cyclophilin-cyclosporine-contacts-calcineurin-active-site","predicate":"contacts_active_site_of","statement":"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.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"78d7edbd-eb27-5151-90e4-73a1ce2b3ebe","mechanism_event_label":"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 in","subject":{"id":"90dbcd2a-88d9-5a7f-85b2-5372761d4b4e","slug":"cyclophilin-a-cyclosporine","display_name":"Cyclophilin A-cyclosporine complex","entity_type_key":"protein_complex"},"object":{"id":"27eef74a-1d9b-57b3-a245-82d452d6cb54","slug":"calcineurin","display_name":"Calcineurin","entity_type_key":"protein_complex"},"evidence_count":1,"mechanism_event":{"id":"78d7edbd-eb27-5151-90e4-73a1ce2b3ebe","stable_key":"1bbf9d44-8d2b-5b35-8f82-f6876558b0b3:cyclophilin-cyclosporine-contacts-calcineurin-active-site-event","event_type":"biochemical_relationship","label":"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 in","description":"Calcineurin catalytic and regulatory subunit interface","status":"provisional","compartment":null,"participants":[{"entity":{"id":"90dbcd2a-88d9-5a7f-85b2-5372761d4b4e","slug":"cyclophilin-a-cyclosporine","display_name":"Cyclophilin A-cyclosporine complex","entity_type_key":"protein_complex"},"role":"acting component","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"27eef74a-1d9b-57b3-a245-82d452d6cb54","slug":"calcineurin","display_name":"Calcineurin","entity_type_key":"protein_complex"},"role":"component the finding is about","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"duration","value_text":"Not applicable","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"evidence_access","value_text":"Primary PubMed abstract and indexed metadata reviewed. 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No direction is recorded for this claim, because a binding geometry is not itself an increase or a decrease.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Recombinant human proteins in crystal","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"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.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. 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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.","file_path":"","sha256":"499d00555a629cba2271c3888d7e93627949891d565c4c78c843610de2913080","revision_id":"263ee68a-4184-51d0-a977-197d7ddb7a4d","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}