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. 2017 Aug 18;7:8776. doi: 10.1038/s41598-017-07141-8

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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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Recognition of the residue at the subsite −3 in substrate peptides. Interaction between human TPST1 and the residue at the −3 position in (a) C4P5Y5 and (b) the gastrin peptide productive form. (c) Interaction between human TPST1 and the sulfated tyrosine residue at the subsite −3 in the C4P5Y5 model peptide. The sulfotyrosine residue at the subsite −3 in C4P5Y5 is recognized by human TPST1 through electrostatic and hydrophobic interactions. Hydrogen bonds are depicted as orange dotted lines.