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首页> 美国卫生研究院文献>other >EQUILIBRIUM UNFOLDING OF THE RETINOID X RECEPTOR LIGAND BINDING DOMAIN AND CHARACTERIZATION OF AN UNFOLDING INTERMEDIATE†*
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EQUILIBRIUM UNFOLDING OF THE RETINOID X RECEPTOR LIGAND BINDING DOMAIN AND CHARACTERIZATION OF AN UNFOLDING INTERMEDIATE†*

机译：类视黄醇X受体配体结合域的平衡解折叠和非折叠中间体的特征†*

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摘要

The retinoid X receptor (RXR) is a ligand-activated transcription factor that plays an important role in growth and development and the maintenance of cellular homeostasis. A thermodynamic ultraviolet circular dichroism, tryptophan fluorescence and ligand binding activity with guanidine as a chemical denaturant is consistent with a two step mechanism. The dimeric LBD equilibrates with a monomeric intermediate (ΔG0(H2O) equal to 8.3 kcal/mol) that is in equilibrium with the unfolded state (ΔG0(H2O) equal to 2.8 kcal/mol). The intermediate was characterized by analytical ultracentrifugation, spectroscopy, and collisional fluorescence quenching, which imply that the monomeric intermediate maintains a high degree, but not all, of native secondary structure. Although intrinsic fluorescence from native and intermediate suggests little change in tryptophan environments, fluorescence intensities from fluorescein reporter groups differ significantly between the two structures. Analysis of the collisional quenching results imply that the intermediate is characterized by tryptophans with increased accessibility to small solutes and less overall compactness than the native protein.
机译：类视黄醇X受体（RXR）是一种配体激活的转录因子，在生长发育和维持细胞稳态中起着重要作用。用胍作为化学变性剂的热力学紫外圆二色性，色氨酸荧光和配体结合活性与两步机理一致。二聚体LBD与单体中间体（ΔG 0 （H2O）等于8.3 kcal / mol）平衡，该单体中间体处于未折叠状态（ΔG 0 （H2O）等于至2.8 kcal / mol）。该中间体通过分析超速离心，光谱学和碰撞荧光猝灭来表征，这暗示该单体中间体保持了高度但不是全部的天然二级结构。尽管来自天然和中间体的固有荧光表明色氨酸环境几乎没有变化，但是来自荧光素报告基团的荧光强度在两个结构之间存在显着差异。碰撞猝灭的分析表明该中间体的特征在于色氨酸，与天然蛋白质相比，色氨酸具有更高的可与小溶质接触的能力，且整体紧密度更低。

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