Jump to main content
Jump to site search

Issue 73, 2013
Previous Article Next Article

Crosstalk between Cu(i) and Zn(ii) homeostasis via Atx1 and cognate domains

Author affiliations

Abstract

The copper metallochaperone Atx1 and the N-terminal metal-binding domain of a copper-transporting ATP-ase can form tight Zn(II)-mediated hetero-complexes in both cyanobacteria and humans. Copper and zinc homeostasis could be linked by metal binding to these CXXC-containing proteins.

Graphical abstract: Crosstalk between Cu(i) and Zn(ii) homeostasis via Atx1 and cognate domains

Back to tab navigation

Supplementary files

Publication details

The article was received on 12 Apr 2013, accepted on 24 Jul 2013 and first published on 25 Jul 2013


Article type: Communication
DOI: 10.1039/C3CC42709A
Chem. Commun., 2013,49, 8000-8002
  • Open access: Creative Commons BY license
  •   Request permissions

    Crosstalk between Cu(I) and Zn(II) homeostasis via Atx1 and cognate domains

    A. Badarau, A. Baslé, S. J. Firbank and C. Dennison, Chem. Commun., 2013, 49, 8000
    DOI: 10.1039/C3CC42709A

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements