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. 2017 Sep 5;8:430. doi: 10.1038/s41467-017-00572-x

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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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Fig. 4 — Side-by-side comparison with key features in the PvPKG/ML1 and PvPKG/ML10 co-structures. a Hydrogen bonds provide key interactions: At the hinge of the kinase domain, V614 forms hydrogen bonds with the amino-pyrimidine group of both ML1 (left) and ML10 (right). In addition, ML10 extends a sulfonamide moiety to form hydrogen bonds with D675 and F676, resulting in significantly greater inhibitory potency than ML1. b Gatekeeper confers specificity: Both ML1 (left) and ML10 (right) extend a fluorophenyl group to occupy a hydrophobic pocket adjacent to T611 (magenta). This explains in part the specificity of the inhibitors as a residue with a longer side-chain may potentially clash with this functional group. c Hydrophobic network enhances inhibitory potency: Plasmodium PKG also interacts with both ML1 (left) and ML10 using a network of hydrophobic residues (see Supplementary Fig. 13 for the same figure with amino-acid labels)

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