X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex

@article{Griffith1995XraySO,
  title={X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex},
  author={James P. Griffith and Joseph L. Kim and Eunice EunKyeong Kim and Michael D. Sintchak and John A. Thomson and Matthew J. Fitzgibbon and Mark A. Fleming and Paul R. Caron and Kathy Hsiao and Manuel A. Navia},
  journal={Cell},
  year={1995},
  volume={82},
  pages={507-522}
}

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References

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Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex
The structure of the human FK506 binding protein (FKBP), complexed with the immunosuppressant FK506, has been determined to 1.7 angstroms resolution by x-ray crystallography. The conformation of the
Characterization of the calcium‐binding sites of calcineurin B
Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin.
TLDR
It is suggested that immunosuppressive ligands express their differential effects in part by modulating the conformation of FKBP12, in agreement with mutagenesis experiments on the protein, and not simply through differences in the ligand structures themselves.
Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin.
TLDR
High resolution structures for the complexes formed by the immunosuppressive agents FK506 and rapamycin with the human immunophilin FKBP-12 have been determined by X-ray diffraction and suggest ways in which this catalytic activity could operate.
Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A.
TLDR
The results show that calcineurin is a target of drug-immunophilin complexes in vivo and establish a physiological role for calcium-dependent serine/threonine phosphatase in T-cell activation.
Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
TLDR
It is reported here that overexpression of calcineurin in Jurkat cells renders them more resistant to the effects of CsA and FK506 and augments both NFAT- and NFIL2A-dependent transcription.
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