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The Ras superfamily of small GTPases are guanine-nucleotide-dependent switches essential for numerous cellular processes. Mutations or dysregulation of these proteins are associated with many diseases, but unsuccessful attempts to target the small GTPases directly have resulted in them being classed as "undruggable". The GTP-dependent signaling of these proteins is controlled by their regulators; guanine nucleotide exchange factors (GEFs), GTPase activating proteins (GAPs), and in the Rho and Rab subfamilies, guanine nucleotide dissociation inhibitors (GDIs). This review covers the recent small molecule and biologics strategies to target the small GTPases through their regulators. It seeks to critically re-evaluate recent chemical biology practice, such as the presence of PAINs motifs and the cell-based readout using compounds that are weakly potent or of unknown specificity. It highlights the vast scope of potential approaches for targeting the small GTPases in the future through their regulatory proteins.

Original publication

DOI

10.1002/anie.201900585

Type

Journal article

Journal

Angew Chem Int Ed Engl

Publication Date

16/04/2020

Volume

59

Pages

6342 - 6366

Keywords

drug discovery, peptides, protein-protein interactions, small GTPases, small molecules, Binding Sites, Drug Evaluation, Preclinical, Humans, Molecular Dynamics Simulation, Monomeric GTP-Binding Proteins, Peptides, Phylogeny, Protein Binding, Small Molecule Libraries, Structure-Activity Relationship