Understanding the molecular details of catalysis in a proline isomerase
Research area: Computational Structural Biology
Associate members: Andrea Cavalli
Status: In progress
Cyclophilins are a part of the ubiquitous family of enzymes which catalyses the isomerisation transition between peptidyl and prolyl conformations, which plays a crucial role in the folding of many proteins. However, these enzymes have also been identified as a putative drug-target to treat a number of diseases, including viral infections such as Hepatitis C.
In this project we wish to understand the molecular details of the catalysis of Cyclophilin A, and in particular also the inhibition of this function. To this end, we are collaborating with the group Prof. Riek at the ETH in Zürich to analyse high-resolution exact nuclear Overhauser enhancement data and residual dipolar coupling data on Cyclophilin A in complex with cyclosporin, which is known inhibitor of its function, and in absence of this inhibitor.