Probing immunosuppressant action with a nonnatural immunophilin ligand

@article{Bierer1990ProbingIA,
  title={Probing immunosuppressant action with a nonnatural immunophilin ligand},
  author={Barbara E. Bierer and Patricia K. Somers and Thomas J. Wandless and Steven J. Burakoff and Stuart L. Schreiber},
  journal={Science},
  year={1990},
  volume={250},
  pages={556 - 559}
}
The immunosuppressants FK506 and rapamycin bind to the same immunophilin, FK506 binding protein (FKBP), and inhibit distinct signal transduction pathways in T lymphocytes. A nonnatural immunophilin ligand, 506BD, which contains only the common structural elements of FK506 and rapamycin, was synthesized and found to be a high-affinity ligand of FKBP and a potent inhibitor of FKBP rotamase activity. Whereas 506BD does not interfere with T cell activation, it does block the immunosuppressive… Expand
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