Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Biometals. 2007 Jun;20(3-4):275-89. Epub 2007 Jan 16.

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

Author information

  • 1Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich, NR4 7TJ, UK.

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 P(1B)-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.

PMID:
17225061
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Write to the Help Desk