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. 2017 Aug 8;7:7501. doi: 10.1038/s41598-017-07755-y

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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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Active VRKs, PLK1 and RSK2 have dissimilar binding modes to pteridinone compounds. (a,b) BI-D1870 has two distinct binding modes to VRK1, supported by different interactions with the protein hinge region. (c) BI-D1870 interaction with VRK2. Both VRK1 and VRK2 are constitutively in a DFG-in, active conformation. (d) RSK2 binds to BI-D1870 in an inactive, DFG-out conformation (PDB:5DK9). (e) BI-D2536 binding mode to PLK1 (PDB:2RKU) is similar to pose 2 in VRK1_3-364/BI-D1870 co-crystals. PLK1 residues at the back of the ATP-binding site (K82, E101 and D194) contact the compound via an extensive network of water-mediated hydrogen bonds. Side chains of Asp and Tyr/Phe residues from the DFG (DYG in the VRKs) are shown in stick representations; Cαs in these residues are shown as spheres (salmon).