ePrints

Copper chaperones: function, structure and copper-binding properties

Lookup NU author(s): Dr Dr MD Harrison Harrison

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

Copper is an absolute requirement for living systems and the intracellular trafficking of this metal to copper-dependent proteins is fundamental to normal cellular metabolism. The copper chaperones perform the dual functions of trafficking and the prevention of cytoplasmic exposure to copper ions in transit. Only a small number of copper chaperones have been identified at this time but their conservation across plant, bacterial and animal species suggests that the majority of living systems utilise these proteins for copper routing. The available data suggest that each copper-dependent protein in the cell is served by a specific copper chaperone. Although copper chaperones cannot be substituted for one another in a given cell type, copper chaperones that deliver to the same protein in different cell types appear to be functionally equivalent. The majority of the copper chaperones identified thus far have an

Publication metadata

Author(s): Harrison MD, Jones CE, Dameron CT

Publication type: Article

Publication status: Published

Journal: Journal of Biological Inorganic Chemistry

Year: 1999

Volume: 4

Issue: 2

Pages: 145-153

Print publication date: 01/01/1999

ISSN (print): 0949-8257

ISSN (electronic): 1432-1327

Publisher: Springer

URL: http://dx.doi.org/ 10.1007/s007750050297

DOI: 10.1007/s007750050297

Altmetrics

Share