Allosteric targeting of receptor tyrosine kinases

Nat Biotechnol. 2014 Nov;32(11):1113-20. doi: 10.1038/nbt.3028.

Abstract

The drug discovery landscape has been transformed over the past decade by the discovery of allosteric modulators of all major mammalian receptor superfamilies. Allosteric ligands are a rich potential source of drugs and drug targets with clear therapeutic advantages. G protein-coupled receptors, ligand-gated ion channels and intracellular nuclear hormone receptors have all been targeted by allosteric modulators. More recently, a receptor tyrosine kinase (RTK) has been targeted by an extracellular small-molecule allosteric modulator. Allosteric mechanisms of structurally distinct molecules that target the various receptor families are more alike than originally anticipated and include selectivity, orthosteric probe dependence and pathway-biased signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation / drug effects
  • Animals
  • Drug Discovery
  • Humans
  • Ligand-Gated Ion Channels / genetics
  • Ligand-Gated Ion Channels / metabolism*
  • Receptor Protein-Tyrosine Kinases / genetics
  • Receptor Protein-Tyrosine Kinases / metabolism*
  • Receptors, Cytoplasmic and Nuclear / genetics
  • Receptors, Cytoplasmic and Nuclear / metabolism*
  • Receptors, G-Protein-Coupled / genetics
  • Receptors, G-Protein-Coupled / metabolism*
  • Signal Transduction / drug effects
  • Small Molecule Libraries / pharmacology

Substances

  • Ligand-Gated Ion Channels
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, G-Protein-Coupled
  • Small Molecule Libraries
  • Receptor Protein-Tyrosine Kinases