- Protein Classification
- Protein Links
| 1cwa » Cyclosporin | |
|---|---|
| Hydrophobic Thickness or Depth | 10.2 ± 2.5 Å |
| Tilt Angle | 82 ± 53° |
| ΔGtransfer | -7.2 kcal/mol |
| Links to 1cwa | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | out |
| Resolution | 2.1 Å |
| Other PDB entries of this protein | none |
| Number of subunits | 1 |
| Experimental Verification for 1cwa » Cyclosporin |
|---|
| This conformation of cyclosporine was taken from a complex with cyclophilin (1cwa) where all its hydrophobic side chains are exposed to the outside medium and the structure of the polypeptide backbone is non-regular. The peptide adopts a competely different conformation (beta-hairpin) with partially buried nonpolar side-chains in organic solvents and probably in water (Wuthrich et al. 1991). Therefore, the calculated transfer energy is strongly overestimated and may be irrelevant (experimental value is -7.4 kcal/mol, Schote et al. 2002). |
| 2 references |
|---|
| Schote, U., Ganz, P., Fahr, A., and Seelig, J. 2002. Interactions of cyclosporines with lipid membranes as studied by solid-state nuclear magnetic resonance spectroscopy and high-sensitivity titration calorimetry. J. Pharm. Sci. 91:856-867. PubMed |
| Wuthrich K, von Freyberg B, Weber C, Wider G, Traber R, Widmer H, Braun W. 1991. Receptor-induced conformation change of the immunosuppressant cyclosporin A. Science 254:953-954. PubMed |
