Copper chaperone for superoxide dismutase (CCS)

Copper chaperone for superoxide dismutase (CCS) is a specialized **metallochaperone protein** that binds and delivers copper(I) ions specifically to the copper/zinc superoxide dismutase (SOD1) enzyme in the cytoplasm and other cell compartments[3][2][5]. CCS is essential for the post-translational activation of SOD1 by inserting copper into its active site, a step crucial for SOD1’s antioxidant function in converting superoxide radicals to oxygen and hydrogen peroxide. CCS is organized into three domains: an N-terminal domain homologous to Atx1 (for copper acquisition), a central domain homologous to SOD1 (for specific interaction with SOD1), and a C-terminal domain containing a CXC motif required for the transfer of copper to SOD1[5][3]. CCS is critical for copper homeostasis and protection from oxidative stress in eukaryotic cells, and its dysfunction or absence impairs SOD1 activity, increasing vulnerability to oxidative damage—particularly relevant in the pathogenesis of neurodegenerative disorders such as ALS[4][1][5]. **Note:** - The protein is well-characterized as a molecular chaperone and not a receptor, enzyme, transporter, or transcription factor. - CCS itself is not a common direct therapeutic target but is central in copper metabolism and redox biology[5][4]. - No evidence indicates this is a misspelled or incorrect target name. - Most references use "CCS" as the canonical abbreviation for this protein[2][5].

Other names

Copper chaperone for SODCCSCu chaperone for SOD1Cu chaperone for superoxide dismutase 1SOD chaperone

Facilitation of copper(I) delivery to apo-superoxide dismutase 1 (SOD1); Ensures safe intracellular copper trafficking, preventing toxic effects of free copper; Promotes proper folding and activation of SOD1