Probing with tool molecules, and by modeling and X-ray crystallography the binding modes of two structurally distinct series of DPP-4 inhibitors led to the discovery of a rare aromatic fluorine H-bond and the spatial requirement for better biaryl binding in the DPP-4 enzyme active site. These newly found binding elements were successfully incorporated into novel DPP-4 inhibitors.
        
Representative scheme of DPP4N_Peptidase_S9 structure and an image from PDBsum server
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Databases
PDB-Sum
3D4L Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
3D4LFold classification based on Structure-Structure alignment of Proteins - FSSP server