1ikf
From Proteopedia
A CONFORMATION OF CYCLOSPORIN A IN AQUEOUS ENVIRONMENT REVEALED BY THE X-RAY STRUCTURE OF A CYCLOSPORIN-FAB COMPLEX
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
A conformation of cyclosporin A in aqueous environment revealed by the X-ray structure of a cyclosporin-Fab complex., Altschuh D, Vix O, Rees B, Thierry JC, Science. 1992 Apr 3;256(5053):92-4. PMID:1566062 Page seeded by OCA on Fri May 2 20:05:57 2008
