Solution Conformation of a Cyclophilin-Bound Proline Isomerase Substrate

Lazaros T. Kakalis, Ian M. Armitage

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


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° out of planarity.

Original languageEnglish (US)
Pages (from-to)1495-1501
Number of pages7
Issue number6
StatePublished - Feb 1 1994


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