Crystal structure of an RNA aptamer protein complex at 2.8 Å resolution
Crystal structure of an RNA aptamer protein complex at 2.8 Å resolution
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DOI：
10.1038/nsb0298-133
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发表时间：
1998-02-01
期刊：
影响因子：
--
通讯作者：
Stockley, PG
中科院分区：
文献类型：
--
作者：
Convery, MA;Rowsell, S;Stockley, PG
与噬菌体 MS2 外壳蛋白结合的 RNA 适体的晶体结构（分辨率为 2.8 埃）已被确定，它提供了一个机会来比较 MS2 外壳蛋白和野生型操纵子与适体之间的相互作用，适体的二级结构与野生型 RNA 的不同之处在于具有一个三碱基环（与四环相比）以及该环与序列特异性识别元件之间的额外碱基对。 在茎中，RNA 与野生型操纵子结合在外壳蛋白上的相同位置，并维持许多相同的 RNA-蛋白质相互作用。为了实现这一目标，RNA 茎环经历了 3' 侧的协调重排，同时使 5' 侧和环相互作用基本保持不变，这说明 RNA 具有从不同的一级和二级结构呈现相似分子识别表面的能力。
The crystal structure, at 2.8 Angstrom resolution, of an RNA aptamer bound to bacteriophage MS2 coat protein has been determined, It provides an opportunity to compare the interactions of MS2 coat protein and wild type operator with those of an aptamer, whose secondary structure differs from the wild type RNA in having a three-base loop (compared to a tetraloop) and an additional base pair between this loop and the sequence-specific recognition element in the stem, The RNA binds in the same location on the coat protein as the wild type operator and maintains many of the same RNA-protein interactions. In order to achieve this, the RNA stem loop undergoes a concerted rearrangement of the 3' side while leaving the 5' side and the loop interactions largely unchanged, illustrating the ability of RNA to present similar molecular recognition surfaces from distinct primary and secondary structures.