Mechanism of Ψ-Pro/C-degron recognition by the CRL2
Humans
Ubiquitination
Cryoelectron Microscopy
Ubiquitin-Protein Ligases
/ metabolism
NEDD8 Protein
/ metabolism
Proline
/ metabolism
Protein Multimerization
HEK293 Cells
Protein Binding
Substrate Specificity
Cell Cycle Proteins
/ metabolism
Models, Molecular
Cullin Proteins
/ metabolism
Degrons
Receptors, Interleukin-17
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
26 Apr 2024
26 Apr 2024
Historique:
received:
13
10
2023
accepted:
16
04
2024
medline:
27
4
2024
pubmed:
27
4
2024
entrez:
26
4
2024
Statut:
epublish
Résumé
The E3 ligase-degron interaction determines the specificity of the ubiquitin‒proteasome system. We recently discovered that FEM1B, a substrate receptor of Cullin 2-RING ligase (CRL2), recognizes C-degrons containing a C-terminal proline. By solving several cryo-EM structures of CRL2
Identifiants
pubmed: 38670995
doi: 10.1038/s41467-024-47890-5
pii: 10.1038/s41467-024-47890-5
doi:
Substances chimiques
Ubiquitin-Protein Ligases
EC 2.3.2.27
NEDD8 Protein
0
Proline
9DLQ4CIU6V
NEDD8 protein, human
0
IL17RB protein, human
0
Cell Cycle Proteins
0
Cullin Proteins
0
Receptors, Interleukin-17
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3558Informations de copyright
© 2024. The Author(s).
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