Copper chaperones compose a specific class of proteins assuring safe handling and specific delivery of potentially harmful copper ions to a variety of essential copper proteins. Copper chaperones are structurally heterogeneous and can exist in multiple metal-loaded as well as oligomeric forms. Moreover, many copper chaperones can exist in various oxidative states and participate in redox catalysis, connected with their functioning. This review is focused on the analysis of the structural and functional properties of copper chaperones and their partners, which allowed us to define specific regulatory principles in copper metabolism connected with copper-induced conformational control of copper proteins.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.