Basu M, Sen-Majumdar A, Basu A, Murthy U, Das M
J Biol Chem. 1986 Sep 25;261(27):12879-82.
Tyrosine kinase activity of the epidermal growth factor (EGF) receptor can be regulated by its state of association. Studies done with the purified receptor solubilized in Triton X-100 indicate that dimer formation results in negative regulation of kinase, whereas successive binding of EGF and ATP shift the association equilibrium toward the catalytically active monomeric form. The promotion of the monomeric state by ATP can be mimicked by various nonphosphorylating analogs indicating that nucleotide binding rather than autophosphorylation is responsible for stabilizing the monomeric receptor form. Truncated receptor forms, lacking either the external EGF-binding domain or the internal kinase (ATP-binding) domain, are unable to form stable dimers. These results suggest that both intra- and extracellular domains of the receptor act to stabilize the kinase-regulatory dimer.
表皮生长因子（EGF）受体的酪氨酸激酶活性可受其结合状态的调控。对溶解于Triton X - 100中的纯化受体进行的研究表明，二聚体形成会导致激酶的负调控，而EGF和ATP的相继结合会使结合平衡朝着具有催化活性的单体形式移动。ATP对单体状态的促进作用可被各种非磷酸化类似物模拟，这表明核苷酸结合而非自身磷酸化负责稳定单体受体形式。缺少外部EGF结合域或内部激酶（ATP结合）域的截短受体形式无法形成稳定的二聚体。这些结果表明，受体的细胞内和细胞外结构域均起到稳定激酶调节二聚体的作用。
