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. 2018 Sep 12;9:3703. doi: 10.1038/s41467-018-05928-5

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — Structural basis for specificity of Henipavirus W binding to the importin α3. a Importin α3:HeV W structure coloured by conservation of amino acids across all importin α isoforms highlights a 100% conservation in the binding interface. The HeV W NLS backbone (coloured green) is shown in complex with importin α3, with sequence colour rendering red at 30%, white 60%, and blue 100% sequence identity. Figure created in UCSF Chimera using importin α alignments from Clustal Omega. b To identify structural differences, the structures of importin α1:HeV W and importin α3:HeV W were superimposed in UCSF Chimera using MatchEnsemble, and r.m.s.d. plots generated using MatchAlign, and MatchAssess functions. α-helices shown as cylinders; importin α3 coloured orange throughout, and colour conservation rendering for importin α1 set for blue, < 2.5 Å variance, and red for variances > 2.5 Å. Molprobity was used to analyse clash data of importin α3:HeV W NLS superimposed to importin α1, all clashes > 0.8 shown as red crosses. Differences in clash score between importin α1 and α3 are localised to ARMs 7 and 8. Detailed view of clashes are presented in the right box, highlighting residues clashing with the W NLS owing to the difference in positioning of ARMs 7 and 8 in importin α1. All clashing residues are positioned on the α-helices of the ARMs. c Structural comparisons of importin α1 bound to a range of cargo was examined by superimposing the α1:HeV W NLS structure determined in this study (reference molecule, coloured yellow), with importin α1 bound to a monopartite SV40T NLS¹² (1EJL), bipartite Bimax NLS^59,60 (3UKW), and two domain bound structures of CAP80⁶¹ (3FEX, 3FEY) coloured according to r.m.s.d as described in b. Positioning of the α-helices in ARMs 7 and 8 are relatively static across all structures. d Structural comparisons of importin α3 bound to a range of cargo was examined by superimposing the α3:HeV W NLS structure determined in this study (reference molecule coloured orange) with the monopartite RanBP3⁶² (5ZXZ), the NiV W (this study), and domains of PB2¹⁹ (4UAE) and RCC1¹⁵ (5TBK) coloured according to r.m.s.d as described in b. Positioning of α-helices in ARMs 7 and 8 are also relatively static across all structures