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首页> 外文期刊>Biochemistry >Solution Structure and RNA Interactions of the RNA Recognition Motif from Eukaryotic Translation Initiation Factor 4B.
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Solution Structure and RNA Interactions of the RNA Recognition Motif from Eukaryotic Translation Initiation Factor 4B.

机译:真核翻译起始因子4B的RNA识别基序的溶液结构和RNA相互作用。

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摘要

Eukaryotic initiation factor 4B (eIF4B) is a multidomain protein with a range of activities that serves primarily to promote association of messenger RNA to the 40S ribosomal subunit during translation initiation. We report here the solution structure of the eIF4B RNA recognition motif (RRM) domain. It adopts a classical RRM fold, with a betaalphabetabetaalphabeta topology. The most striking difference with other RRM structures is in the disposition of loop 3, which connects the beta2 and beta3 strands and is implicated in RNA recognition. This loop folds down against the body of the RRM and exhibits restricted motion on a milli- to microsecond time scale. Although it contributes to a large basic patch on the RNA binding surface, it does not protrude out from the domain as observed in other RRM structures, possibly implying a different mode of RNA binding. On its own, the core RRM domain provides only a relative weak interaction with RNA targets and appears to require extensions at the N- and C-terminus for high-affinity binding.
机译:真核起始因子4B(eIF4B)是一种多域蛋白,具有一系列活性,主要用于在翻译起始过程中促进信使RNA与40S核糖体亚基的缔合。我们在这里报告eIF4B RNA识别基序(RRM)域的解决方案结构。它采用了经典的RRM折叠,具有betaalphabetabetaalphabeta拓扑。与其他RRM结构最显着的不同之处在于环3的位置,该环连接了beta2和beta3链,并参与RNA识别。该环向RRM的主体向下折叠,并在毫秒到微秒的时间尺度上显示受限的运动。尽管它有助于在RNA结合表面上形成较大的基本补丁,但它不会从域中突出,就像在其他RRM结构中观察到的那样,可能暗示着RNA结合的不同模式。就其本身而言,核心RRM结构域仅提供与RNA靶标的相对弱相互作用,并且似乎需要在N和C端进行延伸以实现高亲和力结合。

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