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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : Acta crystallographica. Section D, Structural biology

Structural evidence for the binding of monocarboxylates and dicarboxylates at pharmacologically relevant extracellular sites of a pentameric ligand-gated ion channel.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section D, Structural biology - 01 Jul 2020

Fourati Z, Sauguet L, Delarue M,

Link to Pubmed [PMID] – 32627739

Link to DOI [DOI] – 10.1107/S205979832000772X

Acta Crystallogr D Struct Biol 2020 Jul; 76(Pt 7): 668-675

GLIC is a bacterial homologue of the pentameric ligand-gated ion channels (pLGICs) that mediate the fast chemical neurotransmission of nerve signalling in eukaryotes. Because the activation and allosteric modulation features are conserved among prokaryotic and eukaryotic pLGICs, GLIC is commonly used as a model to study the allosteric transition and structural pharmacology of pLGICs. It has previously been shown that GLIC is inhibited by some carboxylic acid derivatives. Here, experimental evidence for carboxylate binding to GLIC is provided by solving its X-ray structures with a series of monocarboxylate and dicarboxylate derivatives, and two carboxylate-binding sites are described: (i) the `intersubunit’ site that partially overlaps the canonical pLGIC orthosteric site and (ii) the `intrasubunit’ vestibular site, which is only occupied by a subset of the described derivatives. While the intersubunit site is widely conserved in all pLGICs, the intrasubunit site is only conserved in cationic eukaryotic pLGICs. This study sheds light on the importance of these two extracellular modulation sites as potential drug targets in pLGICs.

https://pubmed.ncbi.nlm.nih.gov/32627739