The structure of human argonaute-2 in complex with miR-20a.
The structure of human argonaute-2 in complex with miR-20a.
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DOI：
10.1016/j.cell.2012.05.017
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发表时间：
2012-07-06
期刊：
影响因子：
64.5
通讯作者：
Joshua-Tor L
中科院分区：
文献类型：
--
作者：
Elkayam E;Kuhn CD;Tocilj A;Haase AD;Greene EM;Hannon GJ;Joshua-Tor L
Argona蛋白是RNA诱导的沉默复合物（RISC）的核心，其中他们使用小的RNA指南识别靶标的靶标。 Ference，混合源自昆虫细胞的RNA对具有生物化学和生物学功能的真核生物蛋白质的结构提供了洞察力，我们报告了与物理上相关的MicroRNA-20A的结构赋予Hago2上的显着稳定性，将这种原本柔性酶锁定在稳定的构象中。
Argonaute proteins lie at the heart of the RNA-induced silencing complex (RISC), wherein they use small RNA guides to recognize targets. Initial insight into the architecture of Argonautes came from studies of prokaryotic proteins, revealing a crescent-shaped base made up of the amino-terminal, PAZ, middle, and PIWI domains. The recently reported crystal structure of human Argonaute-2 (hAgo2), the “slicer” in RNA interference, in complex with a mixed population of RNAs derived from insect cells provides insight into the architecture of a eukaryotic Argonaute protein with defined biochemical and biological functions. Here, we report the structure of human Ago2 bound to a physiologically relevant microRNA, microRNA-20a, at 2.2 Å resolution. The miRNA is anchored at both ends by the Mid and PAZ domains and makes several kinks and turns along the binding groove. Interestingly, miRNA binding confers remarkable stability on hAgo2, locking this otherwise flexible enzyme into a stable conformation.
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DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH
影响因子：
7.2
作者：
Joshua-Tor, Leemor;Hannon, Gregory J.
通讯作者：
Hannon, Gregory J.
影响因子：
64.8
作者：
Lingel, A;Simon, B;Sattler, M
通讯作者：
Sattler, M
影响因子：
64.5
作者：
Mi, Shijun;Cai, Tao;Qi, Yijun
通讯作者：
Qi, Yijun
影响因子：
10.5
作者：
Martinez, J;Tuschl, T
通讯作者：
Tuschl, T