An orthosteric inhibitor of the Ras-Sos interaction

Nat Chem Biol. 2011 Jul 17;7(9):585-7. doi: 10.1038/nchembio.612.

Abstract

Mimics of α-helices on protein surfaces have emerged as powerful reagents for antagonizing protein-protein interactions, which are difficult to target with small molecules. Here we describe the design of a cell-permeable synthetic α-helix, based on the guanine nucleotide exchange factor Sos, that interferes with Ras-Sos interaction and downregulates Ras signaling in response to receptor tyrosine kinase activation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biomimetic Materials / chemical synthesis
  • Biomimetic Materials / chemistry*
  • Biomimetic Materials / pharmacology
  • Biomimetics
  • Cell Line
  • Down-Regulation
  • Drug Design*
  • Humans
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Oligopeptides / pharmacology
  • Protein Interaction Domains and Motifs
  • Protein Structure, Secondary
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Protein-Tyrosine Kinases / chemistry
  • Signal Transduction / drug effects
  • Son of Sevenless Protein, Drosophila / antagonists & inhibitors*
  • Son of Sevenless Protein, Drosophila / chemistry
  • ras Guanine Nucleotide Exchange Factors / antagonists & inhibitors*
  • ras Guanine Nucleotide Exchange Factors / chemistry

Substances

  • Oligopeptides
  • Son of Sevenless Protein, Drosophila
  • ras Guanine Nucleotide Exchange Factors
  • Protein-Tyrosine Kinases