Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor

Masafumi Odaka, Daisuke Kohda, Irit Lax, Joseph Schlessinger, Fuyuhiko Inagaki

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We studied the dimerization of the recombinant soluble extracellular domain of the epidermal growth factor receptor (sEGFR) in response to EGF-binding using multi-angle laser light scattering with size exclusion chromatography (SEC-MALLS). In the absence of EGF, sEGFR behaved as a monomer, However, upon EGF-binding, sEGFR formed a dimer with the stoichiometry of two EGF molecules bound to two sEGFR molecules [(EGF)2-(sEGFR)2]. We analyzed the chemical equilibrium of the dimer formation by SEC-MALLS using a dissociation constant of 0.25 μM for the binding of EGF to sEGFR. The calculated dissociation constant for EGF-induced sEGFR dimerization was found to be 2.4 ± 0.9 μM. These experiments demonstrated that EGF induces receptor dimerization and that two EGF molecules are bound to an EGF-receptor dimer.

Original languageEnglish
Pages (from-to)116-121
Number of pages6
JournalJournal of biochemistry
Issue number1
Publication statusPublished - Jan 1 1997
Externally publishedYes


All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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