Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 432, Issue 10, Pages 3353-3359Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2020.03.021
Keywords
human karyopherin; NLS-binding site; PA-PB1 sub-complex nuclear import; influenza polymerase assembly; host-pathogen interaction
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Funding
- Hofmann-La Roche pRED external collaboration programme
- Agence Nationale pour la Recherche [ANR-14-CE09-0017]
- European Commission (EC) framework program 7 project ComplexINC [279039]
- FRISBI [UMS 3518 CNRS-CEA-UJF-EMBL, ANR-10-INSB-05-02]
- GRAL within the Grenoble Partnership for Structural Biology [ANR-10-LABX-49-01]
- Agence Nationale de la Recherche (ANR) [ANR-14-CE09-0017] Funding Source: Agence Nationale de la Recherche (ANR)
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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-beta subfamily whilst also highlighting differences with the yeast orthologue Kap121p. Moreover, our results provide insight into the structural flexibility of beta-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. (C) 2020 Elsevier Ltd. All rights reserved.
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