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. 2022 Aug 25;13:4988. doi: 10.1038/s41467-022-32655-9

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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. 3 — a Sequence schematic diagrams of integrin subunits α_V and β₈. The headpiece regions of α_V and β₈ used in our study are colored in blue and green, respectively. The other regions of integrin are colored in gray. b Cryo-EM map of the α_Vβ₈/L-TGF-β1 complex. The contour level is 0.384. The integrin subunits are colored as those in a. L-TGF-β1 is colored in orange. The cryo-EM density of LRRC33 is too weak to visualize. c Cartoon presentation of the α_Vβ₈/L-TGF-β1 structure built in the final model. Metal ions in the MIDAS (metal ion-dependent adhesion site) and SyMBS (syngeneic metal ion binding site) are colored in red and purple, respectively. Calcium ions are colored in green. d Ribbon diagram of the interface between α_Vβ₈ and L-TGF-β1_. The side chains of the residues in the integrin-binding region of L-TGF-β1 are shown as sticks, and their cryo-EM densities (contour level of 0.384) are shown as black mesh. The proximal loop and integrin-binding (IB) loop are indicated. e Superposition of our α_Vβ₈/L-TGF-β1 structure with the reported one (PDB code: 6UJA) based on integrin α_Vβ₈. α_Vβ₈ is shown in surface presentation, and L-TGF-β1 is shown in ribbon. L-TGF-β1 in our structure is colored in orange, and that in the reported structure (PDB code: 6UJA) is colored in pink. The side chains of His222 in these two structures are shown as sticks. f, g Detailed comparison of the L-TGF-β1 integrin-binding regions between the two structures shown in e. The residues with distinct conformational changes are shown as sticks. Black dashed lines represent hydrogen bond interaction (<4 Å). h Superposition of the L-TGF-β1 Arm domain between our structure and the reported one (PDB code: 6UJA). The integrin-binding region exhibits a huge conformational difference. Two fixed residues, Ile207 and Asn225, are shown with side chains. i Superposition of our α_Vβ₈/L-TGF-β1 structure with the reported one (PDB code: 6UJA) based on L-TGF-β1. Integrin α_Vβ₈ rotates ~60 degrees along the vertical axis. j Assembled structural model for the 2:2:1 α_Vβ₈/L-TGF-β1/LRRC33 complex. The lower leg of integrin α_V (PDB code: 6AVU) is integrated into this model.