Insulin receptor Arg717 and IGF-1 receptor Arg704 play a key role in ligand binding and in receptor activation.
mutagenesis in vitro
peptide hormone
receptor modification
receptor tyrosine kinase
structure–function
Journal
Open biology
ISSN: 2046-2441
Titre abrégé: Open Biol
Pays: England
ID NLM: 101580419
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
medline:
9
11
2023
pubmed:
8
11
2023
entrez:
7
11
2023
Statut:
ppublish
Résumé
The insulin receptor (IR, with its isoforms IR-A and IR-B) and the insulin-like growth factor 1 receptor (IGF-1R) are related tyrosine kinase receptors. Recently, the portfolio of solved hormone-receptor structures has grown extensively thanks to advancements in cryo-electron microscopy. However, the dynamics of how these receptors transition between their inactive and active state are yet to be fully understood. The C-terminal part of the alpha subunit (
Identifiants
pubmed: 37935358
doi: 10.1098/rsob.230142
pmc: PMC10645074
doi:
Substances chimiques
Receptor, IGF Type 1
EC 2.7.10.1
Receptor, Insulin
EC 2.7.10.1
Insulin-Like Growth Factor I
67763-96-6
Ligands
0
Insulin
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
230142Références
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