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={J. Griffith and J. Kim and E. Kim and M. Sintchak and J. Thomson and M. Fitzgibbon and M. Fleming and P. Caron and K. Hsiao and M. Navia},
  journal={Cell},
  year={1995},
  volume={82},
  pages={507-522}
}
The X-ray structure of the ternary complex of a calcineurin A fragment, calcineurin B, FKBP12, and the immunosuppressant drug FK506 (also known as tacrolimus) has been determined at 2.5 A resolution, providing a description of how FK506 functions at the atomic level. In the structure, the FKBP12-FK506 binary complex does not contact the phosphatase active site on calcineurin A that is more than 10 A removed. Instead, FKBP12-FK506 is so positioned that it can inhibit the dephosphorylation of its… Expand
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  • 179
  • PDF
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  • 645
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  • 212
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  • M. Ivery
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  • Bioorganic & medicinal chemistry
  • 1999
  • 24
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  • 11
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  • 23
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...
1
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References

SHOWING 1-10 OF 89 REFERENCES
The latch region of calcineurin B is involved in both immunosuppressant-immunophilin complex docking and phosphatase activation
  • 103
  • Highly Influential
Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex
  • 527
Characterization of the calcium‐binding sites of calcineurin B
  • 47
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
  • 3,586
  • Highly Influential
Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin.
  • 91
Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin.
  • 1,155
Charged surface residues of FKBP12 participate in formation of the FKBP12-FK506-calcineurin complex.
  • 111
  • PDF
Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A.
  • 701
  • PDF
Conformation of Fk506 in X-Ray Structures of its Complexes with Human Recombinant Fkbp12 Mutants
  • 28
Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
  • 1,546
  • Highly Influential
...
1
2
3
4
5
...