Solution Conformation of a Cyclophilin-Bound Proline Isomerase Substrate
- 15 February 1994
- journal article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 33 (6) , 1495-1501
- https://doi.org/10.1021/bi00172a028
Abstract
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.Keywords
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