Structural and Functional Diversity Among the Members of CTR, the Membrane Copper Transporter Family.
CTR
Copper
Copper Transporter
Journal
The Journal of membrane biology
ISSN: 1432-1424
Titre abrégé: J Membr Biol
Pays: United States
ID NLM: 0211301
Informations de publication
Date de publication:
10 2020
10 2020
Historique:
received:
20
07
2020
accepted:
04
09
2020
pubmed:
26
9
2020
medline:
14
8
2021
entrez:
25
9
2020
Statut:
ppublish
Résumé
Copper is crucial for carrying out normal physiological functions in all higher life forms. Copper Transporter 1 (CTR1) is the high-affinity copper importer found in all eukaryotic organisms. The copper transporter family primarily comprises ~ six members (CTR1-6) and the related members share high sequence homology with CTR. However, with the exception of CTR1, not all six CTRs are present in every organism. Despite having a simple trimeric channel structure, CTR1 and other members exhibit some unique regulatory properties. In the present review, we attempt to understand the diversity and similarity of regulation and functioning of the members of this copper transporter family.
Identifiants
pubmed: 32975619
doi: 10.1007/s00232-020-00139-w
pii: 10.1007/s00232-020-00139-w
pmc: PMC7611187
mid: EMS129497
doi:
Substances chimiques
Copper Transport Proteins
0
Copper
789U1901C5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
459-468Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : DBT-Wellcome Trust India Alliance
ID : IA/I/16/1/502369
Pays : India
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