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. 2021 May 12;22(10):5106. doi: 10.3390/ijms22105106

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Homology modeling of rat $α$ 3 $β$ 4 nAChR and molecular docking of NIC, CLO and ACE. (A,B) Model of the receptor viewed from the membrane plane (A) and from the extracellular domain (B). The protein is shown in cartoon representation with a different color code for each polypeptide. The position of the membrane is represented by spheres. (C–E) Graphical representations of the orthosteric site of rat $α$ 3 $β$ 4 nAChR. The $α$ 3 $β$ 4 subunit interface in complex with: NIC (C); CLO (D); or ACE (E).