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. 2020 Nov 24;11:5964. doi: 10.1038/s41467-020-19617-9

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© The Author(s) 2020

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 — a Cartoon structural representations of KSHV gHgL–LBD and EBV gHgL–LBD. KSHV gH is colored blue in D-I, wheat in D-II, green in D-III, and hotpink in D-IV. EBV gH is colored smudge. KSHV and EBV gL proteins are colored cyan and yellow, respectively. The LBDs of KSHV gHgL–LBD and EBV gHgL–LBD are colored magenta and orange, respectively. b Schematic representation of the KSHV gHgL and EBV gHgL. CT: C-terminal cytoplasmic tail domain, SP: signal peptide, TM: transmembrane. Different colored regions of KSHV gHgL correspond to the different structural domains shown in Fig. 2a. c Superimposition of KSHV gHgL–LBD and EBV gHgL–LBD. KSHV gHgL–LBD and EBV gHgL–LBD are colored as in Fig. 2a. Cartoon diagrams and binding mode pattern are shown. The shift angle and two binding regions of gL to LBD are shown. gL binds to LBD like a fishhook and appressed arm. d, e Binding mode of KSHV gHgL (d) and EBV gHgL (e) to LBD. The surface of LBD is shown, and the channel and peripheral regions of LBD are labeled. The N and C termini of gL are labeled N and C, respectively. f Comparison of the LBD-binding interfaces between KSHV gHgL and EBV gHgL. KSHV gHgL–LBD and EBV gHgL–LBD are colored as in Fig. 2a. The surface of LBD is shown. The LBD-binding residues of KSHV gHgL and EBV gHgL are colored red. The Hloop1, Lloop1–3, and β2 regions of KSHV gHgL are displayed.