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. 2024 Feb 8;15:1201. doi: 10.1038/s41467-024-45505-7

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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 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 — Amino acid sequence of: (a) CXCL12 and locked monomer CXCL12 mutant L55C/I58C (CXCL12-LM) and (b) frHMGB1, frHMGB1-TL and Ac-pep. Basic and acidic residues are shown in blue and red, respectively, nc indicates the net charge. L55C and I58C are colored in cyan on CXCL12 sequences. C22, C44 and C105 are colored in yellow on HMGB1 sequences. On the top of the alignments the elements of secondary structures are indicated. In (a) on the right is reported the cartoon representation of CXCL12 (pdb code: 2KEE), with L55 and I58 explicitly shown in sticks. c Schematic diagram of the fully reduced form of HMGB1 (frHMGB1), tail-less frHMGB1 (frHMGB1-TL), the acidic peptide (Ac-pep) corresponding to the HMGB1 acidic intrinsically disordered region (Ac IDR). BoxA (pink), BoxB (cyan) and Ac IDR (yellow) are represented with boxes and colored on frHMGB1 structure (AF-P63159). The side chains of fully reduced cysteines are represented in red sticks.