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首页> 外文期刊>Journal of Molecular Biology >Inherent Protein Structural Flexibility at the RNA-binding Interface of L30e.
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Inherent Protein Structural Flexibility at the RNA-binding Interface of L30e.

机译：L30e的RNA结合界面处固有的蛋白质结构灵活性。

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摘要

The Saccharomyces cerevisiae ribosomal protein L30 autoregulates its own expression by binding to a purine-rich internal loop in its pre-mRNA and mRNA. NMR studies of L30 and its RNA complex showed that both the internal loop of the RNA as well as a region of the protein become substantially more ordered upon binding. A crystal structure of a maltose binding protein (MBP)-L30 fusion protein with two copies in the asymmetric unit has been determined. The flexible RNA-binding region in the L30 copies has two distinct conformations, one resembles the RNA bound form solved by NMR and the other is unique. Structure prediction algorithms also had difficulty accurately predicting this region, which is consistent with conformational flexibility seen in the NMR and X-ray crystallography studies. Inherent conformational flexibility may be a hallmark of regions involved in intermolecular interactions.
机译：酿酒酵母核糖体蛋白L30通过与其前mRNA和mRNA中富含嘌呤的内部环结合而自动调节其自身表达。对L30及其RNA络合物的NMR研究表明，结合后，RNA的内部环以及蛋白质区域都变得更加有序。已经确定了在不对称单元中具有两个拷贝的麦芽糖结合蛋白（MBP）-L30融合蛋白的晶体结构。 L30拷贝中的柔性RNA结合区具有两个不同的构象，一个类似于通过NMR解析的RNA结合形式，另一个是独特的。结构预测算法也难以准确预测该区域，这与NMR和X射线晶体学研究中观察到的构象灵活性一致。固有的构象柔韧性可能是参与分子间相互作用的区域的标志。

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