We report the synthesis and in vitro activity of a series of novel pyrrolidinyl pyridones and pyrazinones as potent inhibitors of prolyl oligopeptidase (POP). Within this series, compound 39 was co-crystallized within the catalytic site of a human chimeric POP protein which provided a more detailed understanding of how these inhibitors interacted with the key residues within the catalytic pocket.
        
Representative scheme of S9N_PPCE_Peptidase_S9 structure and an image from PDBsum server
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Databases
PDB-Sum
3DDU Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
3DDUFold classification based on Structure-Structure alignment of Proteins - FSSP server