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. 2022 Mar 16;10:823354. doi: 10.3389/fcell.2022.823354

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Copyright © 2022 Zhu, Hu, Bennett, Xu and Mai.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Predicted molecular structural analyses of HN. (A) HN is a small peptide of 24 amino acid residue and is comprised of a poly-leu motif (amino acid residues 9–12). (B) Key residues for BAX binding (amino acid residue 8), IGFBP3 binding (amino acid residues 6–21), and self-dimerization (amino acid residue 7) are shown. The full sequence of HN and its analogue HNG (S14G) with substitution of serine at amino acid residue 14 to glycine are shown. (C) Secondary structure predicts characteristics of a beta-sheet domains (amino acid residues 6–14) and an alpha-helix (amino acid residues 19–24) based on bioinformatic analysis. (D, E) 3D structure analyses are performed using the Phyre2 and (http://www.sbg.bio.ic.ac.uk/phyre2/) (D), and AlphaFold web portals (https://alphafold.ebi.ac.uk/) (E).