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. 2019 Feb 19;10:846. doi: 10.1038/s41467-019-08728-7

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© The Author(s) 2019

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. 1 — The overall fold of VP5. a Cartoon representation of HRPV-2 VP5 (left) and HRPV-6 VP5 (right) coloured from the N-terminal (blue) to the C-terminal (red). Residues Q258 and Q262 connecting the N- and C-terminal domains are shown as green spheres. b Cartoon and topology representation of HRPV-2 VP5 coloured by domains. c Structural differences between the N2 domains of superposed HRPV-2 VP5 (green) and HRPV-6 VP5 (pink). d Localization of the potential fusion peptide depicted as magenta sticks within HRPV-2 VP5 shown as grey cartoon