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. 2021 Sep 1;12:5218. doi: 10.1038/s41467-021-25475-w

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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. 1 — a CD47^BRIL-B6H12 complex structure showing the Fab (light and heavy chains shown as pink and gray cartoon respectively), the ECD (green cartoon), and the TMD helices (helix I, blue; helix II, light green; helix III, orange; helix IV, gray and helix V light orange). The CD47 ECLR is formed by the ECL1 (orange tube), ECL2 (gray tube), and the ¹¹⁷SWF¹¹⁹ loop (green surface shown for W118 and F119). The N-linked glycans are shown as sticks with yellow carbons. The gray lines represent the approximate extracellular and intracellular membrane boundaries. b Close up view of the receptor ECLR showing all the three ECLR loops and important residues (side chains shown as sticks and transparent surfaces). The location of the helical kink in helix I centered on P131 (side chain shown as sticks) is also shown. c Top view of CD47 TMD bundle from the extracellular side showing the position of helices and orientation of the three extracellular loops with respect to the helices. d View of the TM bundle from the intracellular side. The side chain of residues in the IC hydrogen bond network are shown as sticks and labeled.