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首页> 外文期刊>Molecular and Cellular Biology >Inhibition of tyrosine kinase activity of the epidermal growth factor (EGF) receptor by a truncated receptor form that binds to EGF: role for interreceptor interaction in kinase regulation.
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Inhibition of tyrosine kinase activity of the epidermal growth factor (EGF) receptor by a truncated receptor form that binds to EGF: role for interreceptor interaction in kinase regulation.

机译:结合EGF的截短受体形式对表皮生长因子(EGF)受体酪氨酸激酶活性的抑制:受体间相互作用在激酶调节中的作用。

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The tyrosine kinase activity of the epidermal growth factor (EGF) receptor is regulated by a truncated receptor of 100 kilodaltons (kDa) that contains the EGF-binding site but not the kinase domain. The inhibition of kinase is not due to competition for available EGF or for the kinase substrate-binding site. Chemical cross-linking studies suggest that the 100-kDa receptor may form a heterodimer with the intact EGF receptor. Structurally related receptor kinases, such as the platelet-derived growth factor receptor, the insulin receptor, and the Neu receptor, were not inhibited by the 100-kDa receptor. The results indicate that (i) the inhibition was specific for the EGF receptor, (ii) the kinase domain had little or no role in determining target specificity, and (iii) the regulation of kinase may be due to a specific interaction of the 100-kDa receptor with the ligand-binding domain of the EGF receptor kinase.
机译:表皮生长因子(EGF)受体的酪氨酸激酶活性由包含EGF结合位点但不包含激酶结构域的100千道尔顿(kDa)的截短受体调节。激酶的抑制不是由于竞争可用的EGF或竞争激酶底物结合位点。化学交联研究表明100 kDa受体可能与完整的EGF受体形成异二聚体。与结构相关的受体激酶,例如血小板衍生的生长因子受体,胰岛素受体和Neu受体,不受100-kDa受体的抑制。结果表明(i)抑制作用对EGF受体具有特异性,(ii)激酶结构域在确定靶标特异性方面几乎没有作用,或者(iii)激酶的调节可能是由于100的特异性相互作用-kDa受体具有EGF受体激酶的配体结合域。

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