Crystal structures of human calcineurin and the human FKBP12–FK506–calcineurin complex

@article{Kissinger1995CrystalSO,
  title={Crystal structures of human calcineurin and the human FKBP12–FK506–calcineurin complex},
  author={C. Kissinger and H. Parge and D. R. Knighton and C. Lewis and Laura A. Pelletier and A. Tempczyk and V. J. Kalish and K. D. Tucker and R. Showalter and E. W. Moomaw and L. N. Gastinel and N. Habuka and Xinghai Chen and F. Maldonado and J. Barker and R. Bacquet and J. E. Villafranca},
  journal={Nature},
  year={1995},
  volume={378},
  pages={641-644}
}
  • C. Kissinger, H. Parge, +14 authors J. E. Villafranca
  • Published 1995
  • Chemistry, Medicine
  • Nature
  • CALCINEURIN (CaN) is a calcium- and ca 1modulin-dependent protein serine/threonine phosphatase which is critical for several important cellular processes, including T-cell activation1. CaN is the target of the immunosuppressive drugs cyclosporin A and FK506, which inhibit CaN after forming complexes with cyto-plasmic binding proteins (cyclophilin and FKBP12, respectively)2. We report here the crystal structures of full-length human CaN at 2.1 Å resolution and of the complex of human CaN with… CONTINUE READING
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