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. 2022 Sep 20;13:5519. doi: 10.1038/s41467-022-33003-7

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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. 2 — a Cp40-C3b structure solved at 2.0-Å resolution showing a single molecule of Cp40 (stick representation) binding to the β-chain of C3b (green, cartoon representation; the α-chain is shown in cyan). b Cp40 binding site at the MG core of C3b highlighted in red. c Superimposition of the current Cp40-C3b structure (green/cyan) with the previous Cp01-C3c structure (grey). The dotted box shows an enlarged view of the compstatin binding region at the interface of the MG4 and MG5 domains of C3b/C3c. The two compstatin analogs are shown as sticks. d–f Structure of Cp40 in its target-bound conformation. d Cp40 is bound as cyclic 14-amino-acid peptide (green stick representation) engaging in intermolecular contacts with the MG4 (cyan) and MG5 (purple) domains of C3b. e Backbone trace (main chain as cartoon, side chain as sticks) revealing a twisted, O-shaped bound conformation of the disulfide-bridged peptide f Superimposition of Cp01 (grey; from C3c-Cp01 complex) and Cp40 (green; from C3b-Cp40 complex) showing an overall structural similarity with deviations primarily found in side chains not engaging in tight intermolecular interactions. CTC C-terminal complement domain, CUB complement C1r/C1s, Uegf Bmp1 domain, MG macroglobulin domain, TED thioester-containing domain.