Issue 43, 2014

The importance of Zn(ii) binding by the human copper metallochaperone for Cu,Zn-superoxide dismutase

Abstract

The human copper metallochaperone (CCS) for Cu,Zn-superoxide dismutase (SOD1) has a similar Zn(II) site as that in SOD1. Dimeric CCS converts to a monomer in the reduced Zn(II)-free form that weakens the interaction with SOD1. This form of CCS may be fibrillogenic and disease causing, as is the case for demetallated and reduced monomeric SOD1.

Graphical abstract: The importance of Zn(ii) binding by the human copper metallochaperone for Cu,Zn-superoxide dismutase

Supplementary files

Article information

Article type
Communication
Submitted
25 Apr 2014
Accepted
07 May 2014
First published
08 May 2014

RSC Adv., 2014,4, 22542-22544

Author version available

The importance of Zn(II) binding by the human copper metallochaperone for Cu,Zn-superoxide dismutase

S. Allen and C. Dennison, RSC Adv., 2014, 4, 22542 DOI: 10.1039/C4RA03806A

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