ArticleBiophysical journal2026
G12 mutations rewire allosteric communication at the Ras-RalGDS interface.
Article in Biophysical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The Ras subfamily is the most extensively studied branch of the Ras superfamily, with 20% of all human tumors having activating mutations in one of the RAS genes. Recent studies have shown that the Ras/RalGDS/Ral pathway plays a more significant role in the progression of Ras-driven colon and pancreatic cancers than the Ras/Raf and Ras/PI3K pathways. In this study, we investigated the interaction between Ras and the Ras/Rap binding domain (RBD) of RalGDS using long-timescale molecular dynamics simulations. The binding free energy of dimerization showed that Rap1-RBD has the strongest interaction and M-Ras-RBD the weakest interaction among the simulated systems, consistent with experimental results. We noticed that Ras uses the same acidic interface residues when binding to the complementary basic residues of RalGDS and Raf. By analyzing bonding profiles, we identified several conserved interactions across different systems as well as isoform- and mutant-specific preferences. Our results demonstrate that G12D/V mutations favor Glu37-mediated stabilization, specifically through the Glu37
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