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Updated: Jun 25, 2026
14:44
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Three-dimensional structure of the human copper transporter hCTR1
Christopher J De Feo1, Stephen G Aller, Gnana S Siluvai
1Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar Street New Haven, CT 06510, USA.
Summary
The structure of human copper transporter 1 (hCTR1) reveals a trimeric channel essential for cellular copper uptake. This protein binds two copper ions via specific sulfur bonds, crucial for its transport function.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Copper is an essential metal for all eukaryotes, playing vital roles in various cellular processes.
- Copper uptake proteins, such as CTR1, are critical for mediating the acquisition of copper into cells.
Purpose of the Study:
- To determine the high-resolution structure of the human CTR1 protein.
- To elucidate the structural basis of copper binding and transport by hCTR1.
Main Methods:
- Electron crystallography was employed to solve the structure of hCTR1.
- Biochemical assays were used to investigate copper binding and the effects of mutations.
Main Results:
- The structure of trimeric hCTR1 reveals a pore formed at the subunit interfaces, lined by the second transmembrane helix.
- hCTR1 stably binds two Cu(I)-ions through 3-coordinate Cu-S bonds at distinct sites.
- Mutations in a putative binding site altered the copper coordination chemistry.
Conclusions:
- The determined structure provides insights into the mechanism of copper transport by hCTR1.
- hCTR1 functions as a channel with specific copper binding sites crucial for its activity.
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