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Solution conformation of a cyclophilin-bound proline isomerase substrate.

Cyclophilin (CyP) is the 17.8-kDa cytosolic receptor of the immunosuppressant cyclosporin A (CsA) and also a peptidyl prolyl cis-trans isomerase ( PPIase). In order to gain insights into the PPIase mechanism, transferred nuclear Overhauser effect (TRNOE) measurements by two-dimensional 1H NMR were used to determine the conformation of the isomerase-bound standard model substrate suc-AAPF-pNA. Results indicate a cis-like conformation for the CyP-bound substrate with the A-P peptide bond being no more than 40 degrees out of planarity.[1]

References

  1. Solution conformation of a cyclophilin-bound proline isomerase substrate. Kakalis, L.T., Armitage, I.M. Biochemistry (1994) [Pubmed]
 
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