Structure of the agonist 12-HHT in its BLT2 receptor-bound state.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
14 02 2020
14 02 2020
Historique:
received:
22
10
2019
accepted:
28
01
2020
entrez:
16
2
2020
pubmed:
16
2
2020
medline:
18
11
2020
Statut:
epublish
Résumé
G Protein-Coupled receptors represent the main communicating pathway for signals from the outside to the inside of most of eukaryotic cells. They define the largest family of integral membrane receptors at the surface of the cells and constitute the main target of the current drugs on the market. The low affinity leukotriene receptor BLT2 is a receptor involved in pro- and anti-inflammatory pathways and can be activated by various unsaturated fatty acid compounds. We present here the NMR structure of the agonist 12-HHT in its BLT2-bound state and a model of interaction of the ligand with the receptor based on a conformational homology modeling associated with docking simulations. Put into perspective with the data obtained with leukotriene B4, our results illuminate the ligand selectivity of BLT2 and may help define new molecules to modulate the activity of this receptor.
Identifiants
pubmed: 32060341
doi: 10.1038/s41598-020-59571-6
pii: 10.1038/s41598-020-59571-6
pmc: PMC7021728
doi:
Substances chimiques
Fatty Acids, Unsaturated
0
LTB4R2 protein, human
0
Ligands
0
Receptors, Leukotriene B4
0
12-hydroxy-5,8,10-heptadecatrienoic acid
50683-78-8
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2630Références
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