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. 2017 Sep 6;7:10669. doi: 10.1038/s41598-017-10993-9

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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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Deletions in S4–S5 preserve TRPV6 tetrameric assembly and generate non-swapped topology. (a) Sequence alignment of TRPV6* and mutants with deletions in the S4–S5 linker. Leucine L495 is indicated by the red circle. The sequence corresponding to the resolved regions in TRPV6*-Del1 structure is highlighted by yellow. (b) FSEC traces for purified TRPV6* without and with deletions in S4–S5 following tryptophan fluorescence. Note, all samples demonstrate a single monodisperse tetrameric peak. (c) Transmembrane domain of a single TRPV6*-Del1 subunit demonstrates a non-swapped architecture with the characteristic S6-TRP helix connectivity. Blue mesh shows 2Fo-Fc map (1σ). (d) Close-up view of the S4–S5 illustrating boundaries of a missing region (residues 471–485).