X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking - Université Grenoble Alpes Accéder directement au contenu
Article Dans Une Revue Journal of Molecular Biology Année : 2020

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

Résumé

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.
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hal-02555361 , version 1 (23-11-2020)

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Christopher Swale, Bruno da Costa, Laura Sedano, Frederic Garzoni, Andrew Mccarthy, et al.. X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking. Journal of Molecular Biology, 2020, 432 (10), pp.3353-3359. ⟨10.1016/j.jmb.2020.03.021⟩. ⟨hal-02555361⟩
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