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. 2024 Mar 13;15:2284. doi: 10.1038/s41467-024-46624-x

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a Top and side views of VP4 trimers sitting on VP10A (magenta) and VP10B (blue). The three VP4 protomers on VP10A are colored differently and labeled R, S, and T, respectively. b Superimposition of VP4–trimer–VP10A and VP4–trimer–VP10B, revealing that VP4 trimers bind to VP10A and VP10B in a very similar way. c The electrostatic potential of the VP4–VP10 interface, ranging from dark blue (most positive) to deep red (most negative). Positively and negatively charged residues are labeled on VP10 and the VP4 trimer, respectively. Note that the interface on the VP4 trimer is symmetry broken (not C3). d Side view of the VP4 trimer (left) and one protomer (right). VP4 protomers are colored by N-terminal tail (blue), unfurling (red), anchoring (green), and pedestal (gray) domains. Note that α17 of the anchoring domain spans the unfurling domain to connect with the pedestal domain. e Side view of the VP5 trimer (based on PDB ID: 3J9E) of BTV (left) and one protomer (right). VP5 protomers are colored as dagger (blue), unfurling (red), and anchoring (green) domains.