ATPase copper-transporting beta (ATP7B)

ATP7B is a copper-transporting ATPase, also known as ATPase copper-transporting beta. It is a P-type cation transport ATPase and a transporter essential for copper homeostasis. Its primary biological functions include the export of hepatic copper into bile and the transfer of copper to ceruloplasmin, a copper-carrying protein. Dysfunction or mutations in ATP7B are the primary cause of Wilson disease, leading to intracellular copper accumulation in the liver and brain. It is also associated with Wolff syndrome. Therapeutically, D-penicillamine (DPA) and zinc acetate are used to manage Wilson disease by interacting with copper metabolism, though their direct mechanism of action on ATP7B is indirect. Key structural features of ATP7B include six metal-binding domains, transmembrane domains with eight membrane-spanning helices, an actuator domain, a phosphorylation domain, and a nucleotide-binding domain.

Other names

ATP7B