Title : Biosynthesis of Nonimmunosuppressive FK506 Analogues with Antifungal Activity.

Pub. Date : 2019 Aug 23

PMID : 31321978






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Seven new FK506 analogues modified at both the FK506-binding protein 12- and the calcineurin-binding regions were biosynthesized. Tacrolimus FKBP prolyl isomerase 1A Homo sapiens
2 In humans, FK506 binds to FK506-binding protein (FKBP) 12, and the resulting FKBP12-FK506 complex interacts with a Ca2+-calmodulin-dependent phosphatase, calcineurin (CaN). Tacrolimus FKBP prolyl isomerase 1A Homo sapiens
3 In humans, FK506 binds to FK506-binding protein (FKBP) 12, and the resulting FKBP12-FK506 complex interacts with a Ca2+-calmodulin-dependent phosphatase, calcineurin (CaN). Tacrolimus FKBP prolyl isomerase 1A Homo sapiens
4 In humans, FK506 binds to FK506-binding protein (FKBP) 12, and the resulting FKBP12-FK506 complex interacts with a Ca2+-calmodulin-dependent phosphatase, calcineurin (CaN). Tacrolimus FKBP prolyl isomerase 1A Homo sapiens
5 Inactivation of CaN by forming the FKBP12-FK506-CaN ternary complex prevents the activation of nuclear factor of activated T cells (NF-AT), inhibiting the production of interleukin-2 and subsequent T-cell proliferation. Tacrolimus FKBP prolyl isomerase 1A Homo sapiens
6 Therefore, the synthesis of FK506 analogues that can discriminate human FKBP12/CaN from its fungal counterparts may separate antifungal activity from the immunosuppressive activity, thereby allowing the development of a novel antifungal agent. Tacrolimus FKBP prolyl isomerase 1A Homo sapiens