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Updated: Jun 23, 2026
14:44
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces.
Lucia Banci1, Ivano Bertini, Vito Calderone
1Magnetic Resonance Center (CERM), University of Florence, Sesto Fiorentino, Italy.
The Biochemical Journal
|May 21, 2009
Summary
Cellular metal ion balance relies on protein interactions. This study reveals how copper chaperone HAH1 binds to the ATP7A protein, mediated by copper ions, explaining their weak interaction.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Physiology
Background:
- Cellular metal ion homeostasis involves transient protein-protein interactions.
- Metal transfer often occurs via adducts where metal ions bridge interacting proteins.
Purpose of the Study:
- To structurally characterize the interaction between human copper(I)-chaperone HAH1 and the copper-transporting ATPase ATP7A.
- To elucidate the role of metal ions in mediating this protein-protein interaction.
Main Methods:
- Solution-state structural characterization with copper(I).
- X-ray crystallography using cadmium(II) substitution.
- Molecular modeling and site-directed mutagenesis.
Main Results:
- The HAH1-ATP7A interaction involves a small interface (<1000 Ų) with low non-polar atom fraction.
- Metal ions (copper or cadmium) are crucial for adduct formation.
- Electrostatic interactions play a key role in domain selection for adduct formation.
Conclusions:
- The weak affinity between HAH1 and ATP7A is explained by the small, electrostatically driven interaction interface.
- Metal-mediated interactions are critical for specific protein partnerships in metal ion trafficking.
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