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. 2021 Jun 29;12:4012. doi: 10.1038/s41467-021-24184-8

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© The Author(s) 2021

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 Structural comparison of β1 integrins before and after the TS2/16 binding. The β1 subunit portions from the TS2/16-bound α6β1 headpiece (sky blue) and the unbound α5β1 headpiece (PDB ID:4wjk, orange) are superposed at the βI domain and shown as Cα-tracing. TS2/16 Fv-clasp bound to α6β1 is shown as a translucent ribbon diagram. The α2 helix of βI domain harboring TS2/16 epitope residues (N207/K208/V211) and the adjacent α1 helix are labeled. b Metal ion coordination sites in the α6β1 headpiece structure. Simulated-annealing F_o-F_c omit map for metal ions contoured at 2.5 σ is shown in magenta. Ca²⁺ and Mg²⁺ ions assigned in the SyMBS and the MIDAS are shown as green and yellow spheres, respectively. No electron density was observed at the ADMIDAS (dotted circle). c 2F_o-F_c electron density map contoured at 1.2 σ around the ADMIDAS region in the crystal structure of the α6β1-TS2/16 Fv-clasp complex (sky blue), superposed onto the α5β1 headpiece structure (orange) as in a. Ca²⁺ ion bound to the α5β1 headpiece is shown as an orange sphere.