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Science 3 April 1992:
Vol. 256. no. 5053, pp. 92 - 94
DOI: 10.1126/science.1566062
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Articles

Science, Vol 256, Issue 5053, 92-94
Copyright © 1992 by American Association for the Advancement of Science

articles

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

D Altschuh, O Vix, B Rees, and JC Thierry

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 cyclophilin or with the Fab are not identical, these results suggest that the conformation of CsA observed in the bound form preexists in aqueous solution and is not produced by interaction with the proteins.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A Molecular Basis for Different Interactions of Marine Toxins with Protein Phosphatase-1. MOLECULAR MODELS FOR BOUND MOTUPORIN, MICROCYSTINS, OKADAIC ACID, AND CALYCULIN A.
J. R. Bagu, B. D. Sykes, M. M. Craig, and C. F.B. Holmes (1997)
J. Biol. Chem. 272, 5087-5097
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Science. ISSN 0036-8075 (print), 1095-9203 (online)