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John H McGee1,2,3, So Youn Shim2,3,4, Seung-Joo Lee2

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Ras proteins are frequently activated in human cancers, contributing to tumor aggressiveness and therapeutic resistance.
  • Direct inhibition of Ras proteins has been challenging due to the lack of suitable binding pockets on their surface.

Purpose of the Study:

  • To discover and develop novel Ras-binding molecules.
  • To investigate the binding mechanism of these molecules to Ras.
  • To explore new therapeutic strategies targeting Ras proteins.

Main Methods:

  • Screening of a naïve library to identify Ras-binding miniproteins.
  • Protein engineering to enhance miniprotein affinity for Ras.
  • Biochemical assays to characterize miniprotein-Ras interactions.
  • High-resolution crystal structures to determine the binding mode.

Main Results:

  • Discovery of miniproteins with midpicomolar affinity for Ras.
  • Demonstration that miniproteins bind Ras as dimers, inducing an unprecedented conformational change.
  • Identification of a Ras point mutant that stabilizes the open conformation bound by miniproteins.

Conclusions:

  • Miniproteins offer a new class of binders for Ras proteins.
  • The unique binding mode reveals a druggable extended pocket on the Ras effector domain.
  • These findings provide tools for Ras research and enable development of novel Ras inhibitors.