Structures of the entire human opioid receptor family.
GPCRs
analgesics
deltorphin
dynorphin
endogenous opioid peptides
endomorphin
endorphin
ligand selectivity
nociceptin
opioid receptors
Journal
Cell
ISSN: 1097-4172
Titre abrégé: Cell
Pays: United States
ID NLM: 0413066
Informations de publication
Date de publication:
19 01 2023
19 01 2023
Historique:
received:
31
05
2022
revised:
11
10
2022
accepted:
13
12
2022
pubmed:
14
1
2023
medline:
25
1
2023
entrez:
13
1
2023
Statut:
ppublish
Résumé
Opioids are effective analgesics, but their use is beset by serious side effects, including addiction and respiratory depression, which contribute to the ongoing opioid crisis. The human opioid system contains four opioid receptors (μOR, δOR, κOR, and NOPR) and a set of related endogenous opioid peptides (EOPs), which show distinct selectivity toward their respective opioid receptors (ORs). Despite being key to the development of safer analgesics, the mechanisms of molecular recognition and selectivity of EOPs to ORs remain unclear. Here, we systematically characterize the binding of EOPs to ORs and present five structures of EOP-OR-G
Identifiants
pubmed: 36638794
pii: S0092-8674(22)01545-8
doi: 10.1016/j.cell.2022.12.026
pii:
doi:
Substances chimiques
Analgesics, Opioid
0
Opioid Peptides
0
Receptors, Opioid, mu
0
Receptors, Opioid
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
413-427.e17Commentaires et corrections
Type : CommentIn
Informations de copyright
Copyright © 2022 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.