PDB ID or protein name

1cwa » Cyclosporin

1cwa » Cyclosporin
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Topology in Secreted
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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 representing this structure 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