Small pH and Salt Variations Radically Alter the Thermal Stability of Metal-Binding Domains in the Copper Transporter, Wilson Disease Protein

2013 ◽  
Vol 117 (42) ◽  
pp. 13038-13050 ◽  
Author(s):  
Lina Nilsson ◽  
Jörgen Ådén ◽  
Moritz S. Niemiec ◽  
Kwangho Nam ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Thermal Stability ◽  
Metal Binding ◽  
Wilson Disease ◽  
Copper Transporter ◽  
Binding Domains ◽  
Wilson Disease Protein ◽  
Disease Protein ◽  
Thermal Stability Of

scholarly journals Copper relay path through the N-terminus of Wilson disease protein, ATP7B

Metallomics ◽  
2019 ◽  
Vol 11 (9) ◽  
pp. 1472-1480 ◽  
Author(s):  
Kumaravel Ponnandai Shanmugavel ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Metal Binding ◽  
Wilson Disease ◽  
Copper Transport ◽  
Binding Domains ◽  
Wilson Disease Protein ◽  
N Terminus ◽  
Disease Protein ◽  
Yeast Assay

Using a yeast assay, we identified the roles of ATP7B's six metal-binding domains in internal copper transport and soluble chaperone capacity.

scholarly journals Metal Binding Domains 3 and 4 of the Wilson Disease Protein: Solution Structure and Interaction with the Copper(I) Chaperone HAH1†‡

Biochemistry ◽  
2008 ◽  
Vol 47 (28) ◽  
pp. 7423-7429 ◽  
Author(s):  
Lucia Banci ◽  
Ivano Bertini ◽  
Francesca Cantini ◽  
Amy C. Rosenzweig ◽  
Liliya A. Yatsunyk
Keyword(s):  
Metal Binding ◽  
Wilson Disease ◽  
Solution Structure ◽  
Protein Solution ◽  
Binding Domains ◽  
Wilson Disease Protein ◽  
Disease Protein

scholarly journals Disease-causing point-mutations in metal-binding domains of Wilson disease protein decrease stability and increase structural dynamics

BioMetals ◽  
2016 ◽  
Vol 30 (1) ◽  
pp. 27-35 ◽  
Author(s):  
Ranjeet Kumar ◽  
Candan Ariöz ◽  
Yaozong Li ◽  
Niklas Bosaeus ◽  
Sandra Rocha ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Metal Binding ◽  
Wilson Disease ◽  
Point Mutations ◽  
Binding Domains ◽  
Wilson Disease Protein ◽  
Disease Protein

scholarly journals Human copper transporter ATP7B (Wilson disease protein) forms stable dimersin vitroand in cells

2017 ◽  
Vol 292 (46) ◽  
pp. 18760-18774 ◽  
Author(s):  
Samuel Jayakanthan ◽  
Lelita T. Braiterman ◽  
Nesrin M. Hasan ◽  
Vinzenz M. Unger ◽  
Svetlana Lutsenko
Keyword(s):  
Wilson Disease ◽  
Copper Transporter ◽  
Wilson Disease Protein ◽  
Disease Protein ◽  
In Cells

scholarly journals Two forms of Wilson disease protein produced by alternative splicing are localized in distinct cellular compartments

1997 ◽  
Vol 326 (3) ◽  
pp. 897-902 ◽  
Author(s):  
Xiao-Li YANG ◽  
Naoyuki MIURA ◽  
Yoshihiko KAWARADA ◽  
Kunihiko TERADA ◽  
Konstantin PETRUKHIN ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Wilson Disease ◽  
Intracellular Transport ◽  
Copper Metabolism ◽  
Copper Transporter ◽  
Wilson Disease Protein ◽  
Disease Protein ◽  
Human Disorders ◽  
P Type ◽  
Cellular Compartments

Copper is an essential trace element in prokaryotes and eukaryotes and is strictly regulated by biological mechanisms. Menkes and Wilson diseases are human disorders that arise from disruption of the normal process of copper export from the cytosol to the extracellular environment. Recently a gene for Wilson disease (WD) (also named the ATP7B gene) was cloned. This gene encodes a copper transporter of the P-type ATPase. We prepared monoclonal and polyclonal anti-(WD protein) antibodies and characterized the full-length WD protein as well as a shorter form that is produced by alternative splicing in the human brain. We found that the WD protein is localized mainly in the Golgi apparatus, whereas the shorter form is present in the cytosol. These results suggest that the alternative WD proteins act as key regulators of copper metabolism, perhaps by performing distinct roles in the intracellular transport and export of copper.

scholarly journals Probing functional roles of Wilson disease protein (ATP7B) copper-binding domains in yeast

Metallomics ◽  
2017 ◽  
Vol 9 (7) ◽  
pp. 981-988 ◽  
Author(s):  
Kumaravel Ponnandai Shanmugavel ◽  
Dina Petranovic ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Wilson Disease ◽  
Copper Binding ◽  
Functional Roles ◽  
Binding Domains ◽  
Wilson Disease Protein ◽  
Disease Protein

A double deleted yeast system was developed to probe activity of human ATP7B variants in the presence of human Atox1.

Copper-Transfer Mechanism from the Human Chaperone Atox1 to a Metal-Binding Domain of Wilson Disease Protein

2010 ◽  
Vol 114 (10) ◽  
pp. 3698-3706 ◽  
Author(s):  
Agustina Rodriguez-Granillo ◽  
Alejandro Crespo ◽  
Dario A. Estrin ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Metal Binding ◽  
Wilson Disease ◽  
Binding Domain ◽  
Transfer Mechanism ◽  
Wilson Disease Protein ◽  
Metal Binding Domain ◽  
Disease Protein ◽  
Copper Transfer
Sign in / Sign up

Export Citation Format

Share Document