A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.
Journal
Nature chemical biology
ISSN: 1552-4469
Titre abrégé: Nat Chem Biol
Pays: United States
ID NLM: 101231976
Informations de publication
Date de publication:
12 2019
12 2019
Historique:
received:
14
09
2018
accepted:
21
08
2019
pubmed:
9
10
2019
medline:
15
2
2020
entrez:
9
10
2019
Statut:
ppublish
Résumé
Phospholipids are key components of cellular membranes and are emerging as important functional regulators of different membrane proteins, including pentameric ligand-gated ion channels (pLGICs). Here, we take advantage of the prokaryote channel ELIC (Erwinia ligand-gated ion channel) as a model to understand the determinants of phospholipid interactions in this family of receptors. A high-resolution structure of ELIC in a lipid-bound state reveals a phospholipid site at the lower half of pore-forming transmembrane helices M1 and M4 and at a nearby site for neurosteroids, cholesterol or general anesthetics. This site is shaped by an M4-helix kink and a Trp-Arg-Pro triad that is highly conserved in eukaryote GABA
Identifiants
pubmed: 31591563
doi: 10.1038/s41589-019-0369-4
pii: 10.1038/s41589-019-0369-4
pmc: PMC8423587
mid: NIHMS1582778
doi:
Substances chimiques
Ion Channels
0
Ligands
0
Lipids
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1156-1164Subventions
Organisme : NIGMS NIH HHS
ID : P01 GM055876
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM097159
Pays : United States
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