Pub. Date : 2002 Sep
PMID : 12183690
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The polyketides FK506 (tacrolimus) and FK520 (ascomycin) are potent immunosuppressants that function by inhibiting calcineurin phosphatase through formation of an FKBP12-FK506/520-calcineurin ternary complex. | Tacrolimus | FKBP prolyl isomerase 1A | Rattus norvegicus |
| 2 | The polyketides FK506 (tacrolimus) and FK520 (ascomycin) are potent immunosuppressants that function by inhibiting calcineurin phosphatase through formation of an FKBP12-FK506/520-calcineurin ternary complex. | Tacrolimus | FKBP prolyl isomerase 1A | Rattus norvegicus |
| 3 | Based on the crystal structure of the FKBP12-FK506-calcineurin complex, we deduced that the 13- and 15-methoxy groups of FK506 or FK520 are important for inhibition of calcineurin phosphatase but not for binding to FKBP12. | Tacrolimus | FKBP prolyl isomerase 1A | Rattus norvegicus |
| 4 | Based on the crystal structure of the FKBP12-FK506-calcineurin complex, we deduced that the 13- and 15-methoxy groups of FK506 or FK520 are important for inhibition of calcineurin phosphatase but not for binding to FKBP12. | Tacrolimus | FKBP prolyl isomerase 1A | Rattus norvegicus |
| 5 | Based on the crystal structure of the FKBP12-FK506-calcineurin complex, we deduced that the 13- and 15-methoxy groups of FK506 or FK520 are important for inhibition of calcineurin phosphatase but not for binding to FKBP12. | Tacrolimus | FKBP prolyl isomerase 1A | Rattus norvegicus |
| 6 | Based on the crystal structure of the FKBP12-FK506-calcineurin complex, we deduced that the 13- and 15-methoxy groups of FK506 or FK520 are important for inhibition of calcineurin phosphatase but not for binding to FKBP12. | Tacrolimus | FKBP prolyl isomerase 1A | Rattus norvegicus |