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. 2019 Jan 22;9:300. doi: 10.1038/s41598-018-36391-3

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© The Author(s) 2019

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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(a–c) The structure of wild type MUP20 (PDB ID: 2L9C, 6xHis tag is not represented) in different orientations. The 3D representation shows in red the amino acids belonging to the hydrophobic pocket involved in the binding process, according to the LPC/CSU analysis. C-term indicates C-terminus. (d) Relevant residues involved in the ligand-MUP20 interaction. Those in green are conserved across the natural MUP isoforms, while the variable residues are in red. (e) Amino acid mutations in MUP20. The polar/apolar nature of the original and substituted amino acids is reported together with the corresponding hydrophobicity index values (in brackets)³⁶.