Kumar V, Chambon P
Laboratoire de Génétique Moléculaire, des Eucaryotes du CNRS, Strasbourg, France.
Cell. 1988 Oct 7;55(1):145-56. doi: 10.1016/0092-8674(88)90017-7.
Extracts containing wild-type or mutant human estrogen receptor (ER) have been used to study the binding of ER to its responsive element (ERE). Estradiol (E2) or the antiestrogen hydroxytamoxifen is required for ER binding as assayed by gel retardation. The DNA binding domain (DBD) encompasses the highly conserved region C. Both intact ER-E2 complexes and ER mutants truncated for the hormone binding domain (HBD) bind as dimers to an ERE. However, an HBD-truncated ER binds less tightly to an ERE than an intact ER-E2 complex. The DBD and HBD contain a constitutive and a stronger ER-induced dimerization function, respectively. Thus, in addition to inducing the activation function associated with the HBD, estrogen plays a crucial role in the formation of stable ER dimers that bind tightly to ERE.
含有野生型或突变型人雌激素受体（ER）的提取物已被用于研究ER与其反应元件（ERE）的结合。通过凝胶阻滞分析，雌二醇（E2）或抗雌激素羟基他莫昔芬是ER结合所必需的。DNA结合结构域（DBD）包含高度保守的C区域。完整的ER-E2复合物和激素结合结构域（HBD）被截断的ER突变体均以二聚体形式与ERE结合。然而，HBD截断的ER与ERE的结合比完整的ER-E2复合物更松散。DBD和HBD分别包含组成型和更强的ER诱导的二聚化功能。因此，除了诱导与HBD相关的激活功能外，雌激素在形成与ERE紧密结合的稳定ER二聚体中起着关键作用。
