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. 2017 Apr 7;7:725. doi: 10.1038/s41598-017-00732-5

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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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Location of chimeras and mutants to investigate potential orthosteric and allosteric binding sites for AZ10606120. (A) Homology model of the hP2X7R with the three subunits cartoon representations shown in grey, light purple and light pink. Conserved residues are shown as black spheres, residues unique to the P2X7R are shown as red spheres and variant residues between P2X7 and the other subunits are shown as spheres the colour of the subunit they are in. (B) FT site based predictions of orthosteric (teal) and allosteric (raspberry) binding pockets in the P2X7 receptor, conserved residues involved in ATP binding at one subunit interface are shown in black. Panel shows the region highlighted by dotted box in (A). (C) Homology model of the P2X7 receptor (from the side, left and from the top of the receptor, right) showing the region 73–79 (in red) and regions replaced by corresponding region of the P2X1 receptor for the chimeras (colour coding see (D)). Black spheres correspond to the residues that are conserved throughout P2X receptors that co-ordinate the binding of ATP. (D) Amino acid line-up of the extracellular ligand binding region of the human P2X7 and P2X1 receptors. Black residues are conserved in at least one mammalian orthologue of all P2X subunits, red is unique to the P2X7 receptor. Regions of mutation/chimera are shown by coloured boxes.