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Translation01:31

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
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Disease-causing point-mutations in metal-binding domains of Wilson disease protein decrease stability and increase

Ranjeet Kumar1, Candan Ariöz1, Yaozong Li2

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Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
|October 17, 2016
PubMed
Summary

Wilson disease mutations in copper-transporting ATP7B protein destabilize metal-binding domains. This leads to misfolded structures and protein dysfunction, causing Wilson disease.

Keywords:
ATP7BCircular dichroismMetal-binding domainMolecular dynamicsThermal stabilityWilson disease

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Copper (Cu) transport is vital, involving the Wilson disease protein (ATP7B) and its metal-binding domains (MBDs).
  • Wilson disease arises from mutations in ATP7B, particularly within its MBDs, but the biophysical impact remains unclear.

Purpose of the Study:

  • To investigate the in vitro and in silico biophysical consequences of Wilson disease-associated mutations (G85V in MBD1 and G591D in MBD6) within ATP7B's MBDs.
  • To understand how these mutations affect MBD stability, structure, and dynamics.

Main Methods:

  • Investigated clinically-observed Wilson disease mutations G85V and G591D by introducing them into a well-characterized MBD (MBD4).
  • Utilized biophysical techniques to assess thermal stability (unfolding midpoint temperature).
  • Employed molecular dynamics simulations to analyze structural changes and backbone dynamics.

Main Results:

  • Mutations G85V and G591D significantly reduced MBD4 thermal stability, lowering the unfolding midpoint temperature by over 20°C.
  • Mutated MBD4 (MBD4V) adopted a misfolded structure with increased β-sheet content at high temperatures.
  • Molecular dynamics simulations revealed that mutations enhanced backbone fluctuations throughout the MBD.

Conclusions:

  • Reduced stability and increased dynamics of MBD1 or MBD6 are implicated in ATP7B dysfunction in Wilson disease patients.
  • These findings provide a biophysical basis for understanding Wilson disease pathogenesis linked to specific ATP7B mutations.