Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor.
Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor.
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配体结合增强表皮生长因子受体胞外域二聚化的亲和力。
DOI：
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发表时间：
1997
期刊：
影响因子：
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通讯作者：
Fuyuhiko Inagaki
中科院分区：
文献类型：
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作者：
Masafumi Odaka;Daisuke Kohda;I. Lax;J. Schlessinger;Fuyuhiko Inagaki
我们研究了二聚化的重组可溶性细胞外结构域的表皮生长因子受体（sEGFR）在EGF结合反应使用多角度激光散射与尺寸排阻色谱法（SEC-MALLS）。在没有EGF的情况下，sEGFR表现为单体。然而，在EGF结合时，sEGFR形成二聚体，其化学计量为两个EGF分子结合两个sEGFR分子[（EGF）2-（sEGFR）2]。我们使用EGF与sEGFR结合的0.25 μ M解离常数分析了SEC-MALLS二聚体形成的化学平衡。EGF诱导的sEGFR二聚化的计算解离常数为2.4 +/- 0.9 μ M。这些实验表明，EGF诱导受体二聚化，并且两个EGF分子与EGF受体二聚体结合。
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 microM for the binding of EGF to sEGFR. The calculated dissociation constant for EGF-induced sEGFR dimerization was found to be 2.4 +/- 0.9 microM. These experiments demonstrated that EGF induces receptor dimerization and that two EGF molecules are bound to an EGF-receptor dimer.