NMR sample optimization and backbone assignment of a stabilized neurotensin receptor.
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
06 2023
06 2023
Historique:
received:
01
03
2023
revised:
25
04
2023
accepted:
29
04
2023
pmc-release:
01
06
2024
medline:
22
5
2023
pubmed:
5
5
2023
entrez:
4
5
2023
Statut:
ppublish
Résumé
G protein-coupled receptors (GPCRs) are involved in a multitude of cellular signaling cascades and consequently are a prominent target for pharmaceutical drugs. In the past decades, a growing number of high-resolution structures of GPCRs has been solved, providing unprecedented insights into their mode of action. However, knowledge on the dynamical nature of GPCRs is equally important for a better functional understanding, which can be obtained by NMR spectroscopy. Here, we employed a combination of size exclusion chromatography, thermal stability measurements and 2D-NMR experiments for the NMR sample optimization of the stabilized neurotensin receptor type 1 (NTR1) variant HTGH4 bound to the agonist neurotensin. We identified the short-chain lipid di-heptanoyl-glycero-phosphocholine (DH
Identifiants
pubmed: 37142193
pii: S1047-8477(23)00033-3
doi: 10.1016/j.jsb.2023.107970
pmc: PMC10242673
mid: NIHMS1900934
pii:
doi:
Substances chimiques
Receptors, Neurotensin
0
Protons
0
Receptors, G-Protein-Coupled
0
Amides
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
107970Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM129026
Pays : United States
Informations de copyright
Copyright © 2023 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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