X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking.,Journal of Molecular Biology

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X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking.
Journal of Molecular Biology ( IF 4.7 ) Pub Date : 2020-03-25 , DOI: 10.1016/j.jmb.2020.03.021
Christopher Swale ₁ , Bruno Da Costa ₂ , Laura Sedano ₂ , Frédéric Garzoni ₃ , Andrew A McCarthy ₃ , Imre Berger ₄ , Christoph Bieniossek ₅ , Rob W H Ruigrok ₆ , Bernard Delmas ₂ , Thibaut Crépin ₆

Affiliation

Here, we describe the crystal structures of two distinct isoforms of ligand-free human karyopherin RanBP5 and investigate its global propensity to interact with influenza A virus polymerase. Our results confirm the general architecture and mechanism of the IMB3 karyopherin-β subfamily whilst also highlighting differences with the yeast orthologue Kap121p. Moreover, our results provide insight into the structural flexibility of β-importins in the unbound state. Based on docking of a nuclear localisation sequence, point mutations were designed, which suppress influenza PA-PB1 subcomplex binding to RanBP5 in a binary protein complementation assay.

中文翻译：

人类核球蛋白RanBP5的X射线结构，这是流感聚合酶核贩运的重要因素。

在这里，我们描述了无配体的人类核球蛋白RanBP5的两个不同同工型的晶体结构，并研究了其与甲型流感病毒聚合酶相互作用的总体趋势。我们的研究结果证实了IMB3karyopherin-β亚家族的总体结构和机制，同时也强调了与酵母直向同源Kap121p的差异。此外，我们的结果提供了对未结合状态下β-importins的结构灵活性的见解。基于核定位序列的对接，设计了点突变，该突变在二元蛋白互补测定中抑制了流感PA-PB1亚复合体与RanBP5的结合。

更新日期：2020-03-25

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