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. 2020 Mar 27;10:5656. doi: 10.1038/s41598-020-62548-0

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© The Author(s) 2020

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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PGM1-2 has a unique, surface-exposed, highly conserved patch of residues. A conserved FFSIDLK motif (residues 62 to 68, with carbons, nitrogens, and oxygens, as white, dark blue, and dark red, respectively) is unique to PGM1-2. Surface exposed Phe63, Asp66, Leu67, and Lys68 (only conserved as positively charged) are completely conserved in vertebrate PGM1-2 and are ideally located to interact with a PGM1-2 specific binding partner. The PGM1-2 protein is shown as a space-filling CPK calotte model with identical coloring as in Fig. 2a. Domains D4, D3, and D2 are shown in red, pink, and green, respectively. The PGM1-2 isoform specific exon 1-2 encoded segment is shown in light orange/white, while the rest of D1 is colored blue. Parts of the PGM1-2 structure (left) are shown magnified and rotated roughly 50° (top, right) and 80° (bottom, right) around two different axes.