NCOA3 binds ESR1:estrogen:TFGA gene

X-ray crystallography studies illustrated that the ligand-bound ESR1 interacts with LXXLL motif-containing NCOA3 (SRC3) through the ligand-binding domain (LBD) at the C-terminus of ESR1, which also has a ligand-dependent transactivation function (known as AF-2) (Brzozowski et al. 1997). Cryoelectron microscopy (cryo-EM) determined the quaternary structure of an active complex of DNA-bound ESR1, steroid receptor coactivator 3 (SRC3 or NCOA3), and a secondary coactivator (p300/EP300). Structural models suggests the following assembly mechanism for the complex: each of the two ligand-bound ESR1 monomers independently recruits one NCOA3 protein via the transactivation domain of ESR1;the two NCOA3s in turn bind to different regions of one p300 protein through multiple contacts (Yi P et al. 2015).

X射线晶体学研究表明，与配体结合的雌激素受体1（ESR1）通过位于ESR1C端配体结合域（LBD）与包含LXXLL基序的NCOA3（SRC3）相互作用，该区域亦具有配体依赖的转录激活功能（亦称为AF-2）（Brzozowski等人，1997年）。冷冻电子显微镜（cryo-EM）确定了DNA结合的ESR1、类固醇受体共激活因子3（SRC3或NCOA3）及一个次级共激活因子（p300/EP300）的活性复合物的四级结构。结构模型推测该复合物的组装机制如下：两个与配体结合的ESR1单体各自独立通过ESR1的转录激活域招募一个NCOA3蛋白；这两个NCOA3蛋白随后通过多个接触点与一个p300蛋白的不同区域结合（Yi P等人，2015年）。