# name
Active site-directed inhibitors of prolyl oligopeptidase abolishes its conformational dynamics

# metadata.dc.description.abstract[].value
Deciphering conformational dynamics is crucial for understanding the biological functions of proteins and for designing compounds targeting them. In particular, providing an accurate description of microsecond-millisecond motions opens the opportunity for regulating protein-protein interactions (PPIs) by modulating the dynamics of one interacting partner. Here we analyzed the conformational dynamics of prolyl oligopeptidase (POP) and the effects of active-site-directed inhibitors on the dynamics. We used an integrated structural biology approach based on NMR spectroscopy and SAXS experiments complemented by MD simulations. We found that POP is in a slow equilibrium in solution between open and closed conformations, and that inhibitors effectively abolished this equilibrium by stabilizing the enzyme in the closed conformation.

# metadata.dc.source[].value
Articles publicats en revistes (Química Inorgànica i Orgànica)

# metadata.dc.subject.classification[].value
Espectroscòpia de ressonància magnètica nuclear

# metadata.dc.title[].value
Active site-directed inhibitors of prolyl oligopeptidase abolishes its conformational dynamics