Functional properties of the human copper-transporting ATPase ATP7B (the Wilson's disease protein) and regulation by metallochaperone Atox1.

Abstract

Wilson's disease protein (WNDP) is a copper-transporting P(1)-type ATPase which plays a key role in normal distribution of copper in a number of tissues, particularly in the liver and the brain. Copper has numerous effects on WNDP, altering its structure, activity, and intracellular localization. To better understand the function of this copper-transporting ATPase and its regulation by copper, we have recently developed the functional expression systems for WNDP and for Atox1, a cytosolic protein that serves as an intracellular donor of copper for WNDP. Here we summarize the results of our experiments on characterization of the enzymatic properties of WNDP and the effects of Atox1 on the WNDP activity.

• Authors: Svetlana Lutsenko, Ruslan Tsivkovskii, Joel M Walker
• Journal: Annals of the New York Academy of Sciences (Ann N Y Acad Sci) Vol. 986 Pg. 204-11 (Apr 2003) ISSN: 0077-8923 [Print] United States
• PMID: 12763797 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• ATOX1 protein, human
• Cation Transport Proteins
• Copper Transport Proteins
• Metallochaperones
• Molecular Chaperones
• Copper
• Adenosine Triphosphatases
• ATP7B protein, human
• Copper-Transporting ATPases

Topics

• Adenosine Triphosphatases (chemistry, genetics, metabolism)
• Amino Acid Sequence
• Binding Sites
• Catalytic Domain
• Cation Transport Proteins (chemistry, genetics, metabolism)
• Copper (metabolism)
• Copper Transport Proteins
• Copper-Transporting ATPases
• Gene Expression Regulation, Enzymologic
• Hepatolenticular Degeneration (enzymology, genetics)
• Homeostasis
• Humans
• Metallochaperones
• Models, Molecular
• Molecular Chaperones (chemistry, metabolism)
• Protein Structure, Secondary