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

Lookup NU author(s): Stephen Allen, Professor Christopher DennisonORCiD

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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)-depleted form that weakens the interaction with SOD1. This form of CCS may be fibril-logenic and disease causing, as is the case for demetallated and reduced monomeric SOD1.

Publication metadata

Author(s): Allen S, Dennison C

Publication type: Article

Publication status: Published

Journal: RSC Advances

Year: 2014

Volume: 4

Issue: 43

Pages: 22542-22544

Print publication date: 08/05/2014

ISSN (electronic): 2046-2069

Publisher: Royal Society of Chemistry

URL: http://dx.doi.org/10.1039/c4ra03806a

DOI: 10.1039/c4ra03806a

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