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- Probing Transient Copper Chaperone-Wilson Disease Protein Interactions . . .
ent Copper Chaperone-Wilson Disease Protein Interactions at the Single-Molecule Level with Nanovesicle Trapping [J Am Chem S anches directly to two other states The decay constant from each of the six waiting time distributions (i e , τ0f1, τ0f2, τ1f0, τ1f2,
- Probing transient copper chaperone-Wilson disease protein interactions . . .
We observed transient copper chaperone–target protein interactions one event at a time, captured distinct protein interaction intermediates, and resolved intermediate interconversion dynamics
- Structural basis for copper transfer by the metallochaperone for the . . .
The Hah1 metallochaperone protein is implicated in copper delivery to the Menkes and Wilson disease proteins Hah1 and the N-termini of its target proteins belong to a family of metal binding domains characterized by a conserved MT HCXXC sequence motif The crystal structure of Hah1 has been determined in the presence of Cu (I), Hg (II), and Cd
- Probing Weak Copper Chaperone-Wilson Disease Protein Interactions At . . .
It is unclear how the human copper (Cu) chaperone Atox1 delivers Cu to metal-binding domains of Wilson and Menkes disease proteins in the cytoplasm To begin to address this problem, we have characterized Cu (I) release from wild-type Atox1 and two point mutants (Met 10Ala and Lys60Ala)
- Rosenzweig (letter) - ResearchGate
The Hah1 metallochaperone protein is implicated in copper delivery to the Menkes and Wilson disease proteins Hah1 and the N-termini of its target proteins belong to a family of metal binding
- Binding of Copper(I) by the Wilson Disease Protein and Its Copper Chaperone
The Wilson disease protein (WND) is a transport ATPase involved in copper delivery to the secretory pathway Mutations in WND and its homolog, the Menkes protein, lead to genetic disorders of copper metabolism The WND and Menkes proteins are distinguished from other P-type ATPases by the presence of six soluble N-terminal metal-binding domains containing a conserved C XX C metal-binding motif
- PROBING WEAK COPPER CHAPERONE-WILSON DISEASE PROTEIN INTERACTIONS AT . . .
Various pathways for copper transport exist; of particular interest to this thesis is the pathway between the copper chaperone Hah1 and Wilson disease protein (WDP) Limited dynamic information is available on how the copper chaperone Hah1 and the metal binding domains (MBDs) of WDP interact for copper transfer
- Probing functional roles of Wilson disease protein (ATP7B) copper . . .
Abstract After Ctr1-mediated uptake into human cells, copper (Cu) ions are transported by the cytoplasmic Cu chaperone Atox1 to the Wilson disease protein (ATP7B) in the Golgi network Cu transfer occurs via direct protein–protein interactions and leads to incorporation of Cu into Cu-dependent enzymes
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