Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
15 03 2021
15 03 2021
Historique:
received:
24
07
2020
accepted:
17
02
2021
entrez:
16
3
2021
pubmed:
17
3
2021
medline:
1
4
2021
Statut:
epublish
Résumé
The seven 14-3-3 isoforms are highly abundant human proteins encoded by similar yet distinct genes. 14-3-3 proteins recognize phosphorylated motifs within numerous human and viral proteins. Here, we analyze by X-ray crystallography, fluorescence polarization, mutagenesis and fusicoccin-mediated modulation the structural basis and druggability of 14-3-3 binding to four E6 oncoproteins of tumorigenic human papillomaviruses. 14-3-3 isoforms bind variant and mutated phospho-motifs of E6 and unrelated protein RSK1 with different affinities, albeit following an ordered affinity ranking with conserved relative K
Identifiants
pubmed: 33723253
doi: 10.1038/s41467-021-21908-8
pii: 10.1038/s41467-021-21908-8
pmc: PMC7961048
doi:
Substances chimiques
14-3-3 Proteins
0
Phosphoproteins
0
Protein Isoforms
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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