Human glutaredoxin-1 can transfer copper to isolated metal binding domains of the P
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
05 03 2020
05 03 2020
Historique:
received:
03
10
2019
accepted:
15
01
2020
entrez:
7
3
2020
pubmed:
7
3
2020
medline:
18
11
2020
Statut:
epublish
Résumé
Intracellular copper (Cu) in eukaryotic organisms is regulated by homeostatic systems, which rely on the activities of soluble metallochaperones that participate in Cu exchange through highly tuned protein-protein interactions. Recently, the human enzyme glutaredoxin-1 (hGrx1) has been shown to possess Cu metallochaperone activity. The aim of this study was to ascertain whether hGrx1 can act in Cu delivery to the metal binding domains (MBDs) of the P
Identifiants
pubmed: 32139726
doi: 10.1038/s41598-020-60953-z
pii: 10.1038/s41598-020-60953-z
pmc: PMC7057996
doi:
Substances chimiques
ATOX1 protein, human
0
Copper Transport Proteins
0
GLRX protein, human
0
Glutaredoxins
0
Molecular Chaperones
0
Copper
789U1901C5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4157Références
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