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. 2018 Sep 10;9:3668. doi: 10.1038/s41467-018-06078-4

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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. 2 — Structural comparison of the pentonal vertex of α-, β-, and γ-herpesviruses. Surface representations of the pentonal vertex from α- (HSV-1, HSV-2), β- (HCMV), and γ-herpesviruses (KSHV) viewed from the top (a) and bottom (b) are shown. The color scheme is same as Fig. 1c, the β-herpesvirus-specific tegument protein pp150 is colored in purple. Red-colored elliptical lines indicate the UL25-1 C domains that were not modeled because of its flexibility in HSV-2. The major structural differences observed in α-, β-, and γ-herpesviruses are marked by cyan (for VP26 and its homologs), yellow (for VP19C and its homologs) and red boxes (for inner capsid around the interface of Pen1, Pen5, P1, and P6). Enlarged views of the structural differences (boxed) are shown with secondary structural elements colored and labeled. For a and b, rainbow ribbon models show individual proteins (blue N terminus through green and yellow to red C terminus)