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. 2017 Aug 22;7:9146. doi: 10.1038/s41598-017-09629-9

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© The Author(s) 2017

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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Predicted computational tertiary structure of wild-type (WT) and p.Ile38Ser hBEST1 proteins. 4RDQ crystal structure was used as template. (a) Homopentameric structure of WT BEST1 full structure. Red dots represent outer membrane border and blue dots represent intracellular membrane border. Isoleucine 38 position, which is located in the transmembrane (TM) domain 1, is highlighted in red. The yellow box region was magnified in (b) and (c). (b) The side chain of Ile38 in the TM1 domain was described, which consisted of a hydrophobic carbon chain (gray). The side chain protrudes toward the lipid membrane. (c) The side chain of Ser38 presents hydrophilic oxygen residue (red), which may generate a repulsive force with the hydrophobic lipid membrane.