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. 2022 Oct 27;13:6393. doi: 10.1038/s41467-022-34008-y

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© The Author(s) 2022

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. 4 — a The cryo-EM model of gp145 by itself (ectodomain in gray, CHR in orange, and MPER-N in green) with added MPER-C segments from an NMR structure (PDB: 2PV6) showing that the MPERs are membrane-embedded and the distance of the ectodomain (residue Ala662) from the membrane surface is ~10 Å. b Model of gp145 with one 4E10 Fab bound (colored in yellow), showing that the ectodomain is tilted, increasing its distance from the membrane to ~20 Å, and that the MPER-C segment (magenta) must be exposed and oriented approximately perpendicular to the membrane plane (binding mode 1). c Model of gp145 with two 4E10 Fab bound (colored in yellow and gold), showing that the ectodomain remains tilted and that the two Fabs bind very differently. Whereas one Fab shows the same binding mode 1 as in panel (b), the second Fab lifts the MPER-C segment to ~40 Å from the membrane, where it runs approximately parallel to the membrane (binding mode 2); this Fab occupies space normally occupied by the membrane. d Model of gp160 with two bound Fabs of bnAb 10E8 (colored in blue) generated by docking the crystal structure of the 10E8 Fab–MPER epitope complex (PDB: 4U6G) into the cryo-EM map of 10E8 Fab bound to the Env protein of the AMC011 strain (EMDB: 21334). The model shows that the ectodomain is not tilted and yet ~40 Å away from the membrane surface and that both 10E8 Fabs bind MPER-C similar to 4E10 binding mode 1. e Cryo-EM structure of gp145 with three 4E10 Fabs bound (colored in yellow, gold and brown) seen parallel (top) and perpendicular to the membrane plane (bottom). Although binding asymmetrically, all three Fabs show binding mode 2. The color coding is the same as in Figs. 1–3.