| Literature DB >> 29026209 |
Matthieu Schapira1,2, Mike Tyers3,4, Maricel Torrent5, Cheryl H Arrowsmith1,6.
Abstract
Antagonism of protein-protein interactions (PPIs) with small molecules is becoming more feasible as a therapeutic approach. Successful PPI inhibitors tend to target proteins containing deep peptide-binding grooves or pockets rather than the more common large, flat protein interaction surfaces. Here, we review one of the most abundant PPI domains in the human proteome, the WD40 repeat (WDR) domain, which has a central peptide-binding pocket and is a member of the β-propeller domain-containing protein family. Recently, two WDR domain-containing proteins, WDR5 and EED, as well as other β-propeller domains have been successfully targeted by potent, specific, cell-active, drug-like chemical probes. Could WDR domains be a novel target class for drug discovery? Although the research is at an early stage and therefore not clinically validated, cautious optimism is justified, as WDR domain-containing proteins are involved in multiple disease-associated pathways. The druggability and structural diversity of WDR domain binding pockets suggest that understanding how to target this prevalent domain class will open up areas of disease biology that have so far resisted drug discovery efforts.Entities:
Mesh:
Year: 2017 PMID: 29026209 PMCID: PMC5975957 DOI: 10.1038/nrd.2017.179
Source DB: PubMed Journal: Nat Rev Drug Discov ISSN: 1474-1776 Impact factor: 84.694