PPIA
Gene Ontology Biological Process
- RNA-dependent DNA replication [TAS]
- blood coagulation [TAS]
- entry into host cell [TAS]
- establishment of integrated proviral latency [TAS]
- leukocyte migration [TAS]
- lipid particle organization [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of protein secretion [IMP]
- positive regulation of viral genome replication [IMP]
- protein folding [TAS]
- protein peptidyl-prolyl isomerization [IDA]
- regulation of viral genome replication [IMP, TAS]
- uncoating of virus [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral release from host cell [TAS]
- virion assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PPP3CA
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- T cell activation [TAS]
- calcineurin-NFAT signaling cascade [IDA]
- cellular response to drug [IDA]
- dephosphorylation [TAS]
- innate immune response [TAS]
- positive regulation of NFAT protein import into nucleus [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein dephosphorylation [IDA, NAS]
- response to calcium ion [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- calcineurin complex [IDA, NAS]
- cytoplasm [IDA]
- cytosol [TAS]
- nucleoplasm [IDA, TAS]
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes.
Calcineurin, a Ca2+/calmodulin-dependent protein phosphatase, is the common target for two immunophilin-immunosuppressant complexes, cyclophilin A-cyclosporin A (CyPA-CsA) and FKBP-FK506. How the two structurally distinct immunophilin-drug complexes bind the same target has remained unknown. We report the crystal structure of calcineurin (CN) in complex with CyPA-CsA at 2.8-A resolution. The CyPA-CsA complex binds to a composite surface formed by the catalytic ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID