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首页> 外文期刊>Journal of Biomolecular Structure and Dynamics >Trehalose induces functionally active conformation in the intrinsically disordered N-terminal domain of glucocorticoid receptor
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Trehalose induces functionally active conformation in the intrinsically disordered N-terminal domain of glucocorticoid receptor

机译：海藻糖在糖皮质激素受体的本质无序N-末端结构域中诱导功能上有源兼容性

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摘要

Glucocorticoid receptor (GR) is a classic member of the nuclear receptor superfamily and plays pivotal roles in human physiology at the level of gene regulation. Various constellations of cellular cofactors are required to associate with GR to activate/repress genes. The effects of specific ligands on the AF2 structure and consequent preferential binding of co-activators or co-repressors have helped our understanding of the mechanisms involved. But the data so far fall short of fully explaining GR actions. We believe that this is because work so far has largely avoided detailed examination of the contributions of AF1 to overall GR actions. It has been shown that the GR containing only the N-terminal domain (NTD) and the DNA-binding domain (GR500) is constitutively quite active in stimulating transcription from simple promoters. However, we are only beginning to understand structure and functions of GR500 in spite of the fact that AF1 located within the NTD serves as major transactivation domain for GR. Lack of this information has hampered our complete understanding of how GR regulates its target gene(s). The major obstacle in determining GR500 structure has been due to its intrinsically disordered NTD conformation, frequently found in transcription factors. In this study, we tested whether a naturally occurring osmolyte, trehalose, can promote functionally ordered conformation in GR500. Our data show that in the presence of trehalose, GR500 is capable of formation of a native-like functionally folded conformation.
机译：糖皮质激素受体（GR）是核受体超家族的经典构件，在基因调控水平下发挥人体生理学的关键作用。需要各种细胞辅因子的细胞辅因子与GR激活/抑制基因。特定配体对AF2结构的影响以及共激活剂或共压缩机的优先结合有助于我们对所涉及的机制的理解。但到目前为止，数据尚未完全解释GR动作。我们相信这是因为到目前为止的工作已经很大程度上避免了对AF1对整体GR行动的贡献进行了详细的审查。已经表明，仅包含N-末端结构域（NTD）和DNA结合结构域（GR500）的GR在刺激简单启动子刺激转录方面构成思考。但是，我们只是开始了解GR500的结构和功能，尽管AF1位于NTD内作为GR的主要反作用动域。缺乏这些信息阻碍了我们完全了解GR如何调节其靶基因的理解。确定GR500结构的主要障碍是由于其内在无序的NTD构象，经常在转录因子中发现。在这项研究中，我们测试了是否存在天然存在的渗透细胞海藻糖，可以在GR500中促进功能上有序的构象。我们的数据表明，在海藻糖的存在下，GR500能够形成天然的功能折叠构象。

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