Moras D, Gronemeyer H
Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS/INSERM/ULP, Illkirch, France.
Curr Opin Cell Biol. 1998 Jun;10(3):384-91. doi: 10.1016/s0955-0674(98)80015-x.
In the past few years our understanding of nuclear receptor action has dramatically improved as a result of the elucidation of the crystal structures of the empty (apo) ligand-binding domains of the nuclear receptor and of complexes formed by the nuclear receptor's ligand-binding domain bound to agonists and antagonists. Furthermore, the concomitant identification and functional analysis of co-regulators (transcriptional intermediary factors [TIFs], comprising co-activators and co-repressors) previously predicted from squelching studies, have deepened this understanding. Recent data have provided the structural basis for the specific recognition of ligands and the molecular mechanisms of agonism and antagonism, enabling us to gain a comprehensive view of the early steps of nuclear receptor action.
在过去几年中，由于核受体空的（无配体）配体结合结构域以及核受体配体结合结构域与激动剂和拮抗剂形成的复合物的晶体结构得以阐明，我们对核受体作用的理解有了显著提升。此外，先前通过抑制研究预测的共调节因子（转录中介因子[TIFs]，包括共激活因子和共抑制因子）的相继鉴定和功能分析，进一步深化了这一理解。近期的数据为配体的特异性识别以及激动作用和拮抗作用的分子机制提供了结构基础，使我们能够全面了解核受体作用的早期步骤。
