Structural properties of non-traditional drug targets present new challenges for virtual screening.

ABSTRACT: Traditional drug targets have historically included signaling proteins that respond to small molecules and enzymes that use small molecules as substrates. Increasing attention is now being directed toward other types of protein targets, in particular those that exert their function by interacting with nucleic acids or other proteins rather than small-molecule ligands. Here, we systematically compare existing examples of inhibitors of protein-protein interactions to inhibitors of traditional drug targets. While both sets of inhibitors bind with similar potency, we find that the inhibitors of protein-protein interactions typically bury a smaller fraction of their surface area upon binding to their protein targets. The fact that an average atom is less buried suggests that more atoms are need

SUBMITTER: Gowthaman R 

PROVIDER: S-EPMC3819422 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature