A conformation of cyclosporin A in aqueous environment revealed by the X-ray structure of a cyclosporin-Fab complex.

@article{Altschuh1992ACO,
  title={A conformation of cyclosporin A in aqueous environment revealed by the X-ray structure of a cyclosporin-Fab complex.},
  author={Dani{\`e}le Altschuh and O Vix and Bernard Rees and J. C. Thierry},
  journal={Science},
  year={1992},
  volume={256 5053},
  pages={92-4}
}
The conformation of the immunosuppressive drug cyclosporin A (CsA) in a complex with a Fab molecule has been established by crystallographic analysis to 2.65 angstrom resolution. This conformation of CsA is similar to that recently observed in the complex with the rotamase cyclophilin, its binding protein in vivo, and totally different from its conformation in an isolated form as determined from x-ray and nuclear magnetic resonance analysis. Because the surfaces of CsA interacting with… CONTINUE READING

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