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. 2018 Jun 13;16(6):208. doi: 10.3390/md16060208

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© 2018 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 (http://creativecommons.org/licenses/by/4.0/).

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α-Conotoxin binding mode. (A) The acetylcholine binding protein (AChBP) is a soluble homologue of the nAChR ligand binding extracellular domain. AChBP is used extensively as an nAChR surrogate in receptor-ligand structure-activity studies; (B) An overlay of AChBP and ImI, PnIA (A10L, D14K), TxIA, LsIA, BuIA, GIC, PeIA, and LvIA co-crystal structure show a common binding mode at the interface of the principle (+) and complementary (−) subunits; (C) The conserved α-conotoxin residues responsible for anchoring the α-conotoxins in the binding pocket are shown.