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. 2024 May 29;43(14):3009–3026. doi: 10.1038/s44318-024-00128-y

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) The structural model of the α7β1 core displays seven C4BPα (gray) with C4BPβ (blue) inserted in a helix-hairpin-helix conformation with detected DMTMM (black) and DSS (red) cross-links. To highlight C4BPβ involving restraints, C4BPα intra-protein cross-links (except for the K595 self-link) are visualized as semi-transparent. Visualized were the shortest possible cross-links with an allowed 2 Å difference. (B) An overview of the observed XL-MS restraints. XL-MS revealed C4BPβ CCP1 interaction with LG1 of ProS and highlighted the assembly of C4BPα and C4BPβ at the C-terminus of both chains. Intra- (purple), inter- (green), and self- (orange) cross-links of C4BPα (gray), C4BPβ (blue), and ProS (teal) are color-annotated. Visualized were cross-links detected in two out of three experimental replicates. (C) The proposed C4BPβ–ProS interface. The structural model highlights interactions between the C4BPβ CCP3 (blue) and the ProS LG1 (teal) with the DSS cross-links (in red) and resulting interacting residues connected by yellow dashed lines. The generation of the structural models is described below in the full-length glycosylated models of the C4b-binding protein section. Source data are available online for this figure.