Binding of copper(I) by the Wilson disease protein and its copper chaperone (Q24304146)

GOA release 2020-03-11

copper ion binding

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Journal of Biological Chemistry

GOA release 2020-03-11

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3

Amy C Rosenzweig

Amy C

Rosenzweig

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9 December 2023

1

Amy K Wernimont

Amy K

Wernimont

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9 December 2023

Liliya A Yatsunyk

2

Liliya A

Yatsunyk

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9 December 2023

language of work or name

English

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publication date

26 March 2004

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published in

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volume

279

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issue

13

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page(s)

12269-76

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cites work

The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene

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Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase

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The molecular basis of copper homeostasis copper-related disorders

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Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae

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Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis

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HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense

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A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network

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Human copper-transporting ATPase ATP7B (the Wilson's disease protein): biochemical properties and regulation

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CPx-type ATPases: a class of P-type ATPases that pump heavy metals

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The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake

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Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins

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Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution

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Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1

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NMR structure and metal interactions of the CopZ copper chaperone

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Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase

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Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states

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N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat.

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X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines

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The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein

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Functional expression of the menkes disease protein reveals common biochemical mechanisms among the copper-transporting P-type ATPases

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The role of GMXCXXC metal binding sites in the copper-induced redistribution of the Menkes protein

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Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p

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Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein

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Isothermal titration calorimetry of protein-protein interactions

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Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase

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Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase

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Cooperative binding of copper(I) to the metal binding domains in Menkes disease protein

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Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity

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Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae

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Function, structure, and mechanism of intracellular copper trafficking proteins

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The copper toxicosis gene product Murr1 directly interacts with the Wilson disease protein

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Copper-Induced Conformational Changes in the N-Terminal Domain of the Wilson Disease Copper-Transporting ATPase†

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Expression, Purification, and Metal Binding Properties of the N-terminal Domain from the Wilson Disease Putative Copper-transporting ATPase (ATP7B)

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The pH dependence of apparent binding constants between apo-superoxide dismutase and cupric ions

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7 January 2021

Studies on the binding of copper to dopamine beta-monooxygenase and other proteins using the Cu2+ ion-selective electrode

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Copper trafficking: the solution structure of Bacillus subtilis CopZ

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A C-terminal domain of the membrane copper pump Ctr1 exchanges copper(I) with the copper chaperone Atx1

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Cell anchorage permits efficient signal transduction between ras and its downstream kinases

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Characterization of a novel, membrane-bound, 80-kDa matrix-degrading protease from human breast cancer cells. Monoclonal antibody production, isolation, and localization

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Restoration of holoceruloplasmin synthesis in LEC rat after infusion of recombinant adenovirus bearing WND cDNA

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Role of the copper-binding domain in the copper transport function of ATP7B, the P-type ATPase defective in Wilson disease

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7 January 2021

Structure-function analyses of the ATX1 metallochaperone

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Functional analysis of the N-terminal CXXC metal-binding motifs in the human Menkes copper-transporting P-type ATPase expressed in cultured mammalian cells

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Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2

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7 January 2021