Answers are grounded in this paper and cite their sources.
This review highlights allosteric drug design improvements through conformational ensembles in signaling proteins, suggesting enhanced therapeutic strategies.
Proteins involved in signaling networks, such as Ras, mammalian target of rapamycin (mTOR), and epidermal growth factor receptor (EGFR), exist as dynamic conformational ensembles in biomolecular condensates. These ensembles play a crucial role in allosteric drug discovery and action. Traditional approaches in drug discovery often trace back to the induced fit model, which viewed proteins as rigid entities with active and inactive states. However, this model's limitations hindered successful drug development. Advanced molecular dynamics simulations of oncogenic mutants and experiments reveal heterogeneous dynamic ensembles, which can uncover targetable spots like cryptic pockets and cooperative exosites that only exist transiently. In this review, we clarify traditional dogmas and show how recent knowledge improves allosteric drug design by leveraging conformational ensembles, with examples. We further discuss how ensemble-based approaches can advance promising therapeutics, unlocking their potential for more effective future strategies, including in biomolecular condensates.
No takes yet. Share an insight, caveat, or question.
Nussinov et al. (2026) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: