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. 2014 Nov 18;13:434. doi: 10.1186/1475-2875-13-434

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© Kastner et al.; licensee BioMed Central Ltd. 2014

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Protein conformations resulting from molecular docking of active compounds. The antagonist promethazine can bind to D100 in two different conformations. Promethazine exhibits H-bonding to D100 of TM3 and does not interact with either of the serines of TM5 (A) and has potential π -π interactions with either F483 of TM6 or F211 of TM5 (B). The agonist octopamine can potentially H-bond to D100 and S206 (C), S210 (D), or S206, S210, and E161 (E). Octopamine also exhibits potential π -π interactions with either F483 (C) or F484 (D). Note that an H-bond between octopamine and L97 is also seen in panel E, but was ignored as this is a peptide bond and can thus be made with any amino acid. (F) Chemical structures of octopamine and promethazine.