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. 2018 Feb 9;8:2714. doi: 10.1038/s41598-018-21056-y

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© The Author(s) 2018

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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Active site cleft of PmDAP IV and human DPP IV-family enzymes. (A) Superposition of the active site of the Lys-Pro (green) complex of PmDAP IV (magenta) and those of the linagliptin (yellow) complex of human DPP IV (cyan) and ligand-free human FAP (orange). Subsites are indicated by ellipsoids. (B) A schematic figure showing the gliptin-binding sites of PmDAP IV and DPP IV-family enzymes. The diagrams of FAP, DPP IV, and PmDAP IV are drawn based on their crystal structure, whereas that of DPP8/DPP9 is a conceptual diagram.