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. 2022 Jan 21;29:6. doi: 10.1186/s12929-022-00790-6

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© The Author(s) 2022

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — LRG1 protein structure. Schematic representation of LRG1 protein structure. A LRG1 is a 312 aa protein which contains 8 leucine-rich repeats (LRR), 4 N-linked, 1 O-linked glycosylation sites and 2 disulphide bonds. Upon cleavage of the N-terminal signal peptide, LRG1 is released in the extracellular space. The mature form, around 50 kDa, may vary in weight depending on the glycosylation pattern and multimer formation. B LRG1 structure as predicted by ALPHAFOLD2 through deep learning algorithms [223]. β-sheet in green, α-helix in red