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. 2021 Sep 13;22(18):9880. doi: 10.3390/ijms22189880

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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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Predicted binding modes of IMI and THI with the cockroach Pameα7 receptor viewed according to four orientations: from the top of the homomeric pentameric nAChR (top of the A,B); from the side of the C and D subunits (C,D); with the pyridinic ring (left: E,G) and the push-pull fragment (right: F,H), in the plane of the figure, respectively. The docking scores and glide energies computed were −7.2 and −75.1 kcal/mol for IMI and −4.6 and −71.7 kcal/mol for THI, respectively. For clarity, the labelling of the key amino acids involved in intermolecular interactions with the two ligands have been added to (E–G), with these amino acids being represented as ball-and-stick models. For the same reasons, only the polar hydrogen atoms are represented. Tyr: tyrosine, Trp: tryptophan, Val: valine, Asn: asparagine, Lys: lysine.

Predicted binding modes of IMI and THI with the cockroach Pameα7 receptor viewed according to four orientations: from the top of the homomeric pentameric nAChR (top of the A,B); from the side of the C and D subunits (C,D); with the pyridinic ring (left: E,G) and the push-pull fragment (right: F,H), in the plane of the figure, respectively. The docking scores and glide energies computed were −7.2 and −75.1 kcal/mol for IMI and −4.6 and −71.7 kcal/mol for THI, respectively. For clarity, the labelling of the key amino acids involved in intermolecular interactions with the two ligands have been added to (E–G), with these amino acids being represented as ball-and-stick models. For the same reasons, only the polar hydrogen atoms are represented. Tyr: tyrosine, Trp: tryptophan, Val: valine, Asn: asparagine, Lys: lysine.