Atx1-like chaperones and their cognate P-type ATPases:Copper-binding and transfer

Singleton, Chloe and Le Brun, Nick E. (2007) Atx1-like chaperones and their cognate P-type ATPases:Copper-binding and transfer. BioMetals, 20 (3-4). pp. 275-289. ISSN 0966-0844

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Abstract

Copper is an essential yet toxic metal ion. To satisfy cellular requirements, while, at the same time, minimizing toxicity, complex systems of copper trafficking have evolved in all cell types. The best conserved and most widely distributed of these involve Atx1-like chaperones and P1B-type ATPase transporters. Here, we discuss current understanding of how these chaperones bind Cu(I) and transfer it to the Atx1-like N-terminal domains of their cognate transporter.

Item Type:	Article
Uncontrolled Keywords:	atx1,chaperone,copper trafficking,copper transfer,copz,p-type atpase,biomaterials,biochemistry, genetics and molecular biology(all),agricultural and biological sciences(all),metals and alloys ,/dk/atira/pure/subjectarea/asjc/2500/2502
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	18 Jun 2025 08:30
Last Modified:	18 Jun 2025 08:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/99591
DOI:	10.1007/s10534-006-9068-1

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