Abstract
Previous work has shown that these mutations promote tumor growth and ligand-independent EGFR signaling.2 To explore how extracellular missense mutations cause these phenotypes, structural and experimental models of four common extracellular point mutations, A289V, R108K, T263P, and G598V, were generated. Comparison with the wild-type protein suggests that these point mutations promote formation of an elongated, dimerization-ready conformation of the extracellular domain of EGFR in the absence of ligand. Conclusions
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More From: International Journal of Radiation Oncology*Biology*Physics
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