Copper ion binding

Copper ion binding describes the characteristic of certain proteins, peptides, and other molecules to coordinate and interact with copper ions, predominantly in the form of Cu+ (cuprous) or Cu2+ (cupric). This functionality is critical in enzymes (such as cytochrome c oxidase, superoxide dismutase, laccases, and tyrosinases), copper chaperones (such as CCS and ATOX1), and transporters involved in copper homeostasis. The precise binding motif varies: some involve coordination by histidine, methionine, or cysteine residues, often arranged in conserved sequence patterns, and contribute to enzymatic activity, electron transfer, protection from oxidative damage, and protein structure. Dysregulation of copper binding plays roles in genetic and neurodegenerative diseases, and is a target for copper chelation therapy in disorders of copper overload, but "copper ion binding" itself is not a discrete, actionable drug target.

Drugs remove copper from proteins or solution via chelation, or by inhibition of copper transporters/enzymes.