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. 2018 Feb 21;9:304. doi: 10.3389/fimmu.2018.00304

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Copyright © 2018 Loes, Bridgham and Harms.

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 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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MRP-126, as well as mammalian calgranulins, is primarily alpha-helical with a disordered C-terminal extension. (A) Multiple sequence alignment of mammalian calgranulins with chicken MRP-126. Amino acid residues are colored to show sites with similar chemical properties. (B) Homology model of mouse S100A9 (green), opossum S100A9 (blue), and chicken MRP-126 (orange) aligned with human S100A9 (purple) calcium-bound NMR structure PDB: 5i8n. (C) Circular dichroism spectra of mammalian calgranulins and chicken MRP-126.