Ontology highlight
ABSTRACT:
SUBMITTER: Ho TN
PROVIDER: S-EPMC10133702 | biostudies-literature | 2023
REPOSITORIES: biostudies-literature
Ho Thao Nt TN Abraham Nikita N Lewis Richard J RJ
Frontiers in pharmacology 20230413
αD-conotoxins are 11 kDa homodimers that potently inhibit nicotinic acetylcholine receptors (nAChRs) through a non-competitive (allosteric) mechanism. In this study, we describe the allosteric binding mode of the granulin-like C-terminal (CTD) of VxXXB bound to <i>Lymnea stagnalis</i> acetylcholine binding protein (<i>Ls</i>-AChBP), a soluble homologue of the extracellular ligand-binding domain of nAChRs. This co-crystal complex revealed a novel allosteric binding site for nAChR antagonists outs ...[more]