ArticleJournal of the American Chemical Society2011
Model peptides provide new insights into the role of histidine residues as potential ligands in human cellular copper acquisition via Ctr1.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 143 citations in OpenAlex.
- Cu(I) and Cu(II) binding by hyperactive variants of the human CTR1 N-terminus: Insights from cellular and model peptide studies.Journal of inorganic biochemistry · 2026Article
- The molecular basis of the synergistic toxicity of nickel and copper, common environmental co-contaminants.Applied and environmental microbiology · 2025Article
- Human CTR1 Through the Ages: Milestones and Emerging Roles in Disease and Therapy.Biomolecules · 2025Review
- Stability and Pseudocatecholase Activity of Artificial Bis-Histidyl Copper Peptides.Inorganic chemistry · 2025Article
- Biomimetic Pseudopeptides to Decipher the Interplay between Cu and Methionine-Rich Domains in Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Ascorbate: a forgotten component in the cytotoxicity of Cu(II) ATCUN peptide complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- U-shaped nonlinear relationship between dietary copper intake and peripheral neuropathy.Scientific reports · 2024Article
- Reactive Cu2+-peptide intermediates revealed by kinetic studies gain relevance by matching time windows in copper metallomics.Metallomics : integrated biometal science · 2023Article
- Intrinsically disordered ectodomain modulates ion permeation through a metal transporter.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Interactions between copper (II) and β-amyloid peptide using capillary electrophoresis-ICP-MS: Kd measurements at the nanogram scale.Analytical and bioanalytical chemistry · 2022Article
- Dynamical interplay between the human high-affinity copper transporter hCtr1 and its cognate metal ion.Biophysical journal · 2022Article
- A Deeper Insight in Metal Binding to the hCtr1 N-terminus Fragment: Affinity, Speciation and Binding Mode of Binuclear CuInternational journal of molecular sciences · 2022Article
- Multinuclear Metal-Binding Ability of the N-Terminal Region of Human Copper Transporter Ctr1: Dependence Upon pH and Metal Oxidation State.Frontiers in molecular biosciences · 2022Article
- Incorporation of β-Alanine in Cu(II) ATCUN Peptide Complexes Increases ROS Levels, DNA Cleavage and Antiproliferative Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Electrospray-Induced Mass Spectrometry Is Not Suitable for Determination of Peptidic Cu(II) Complexes.Journal of the American Society for Mass Spectrometry · 2021Article
- Designed Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine.iScience · 2020Review
- Key Intermediate Species Reveal the Copper(II)-Exchange Pathway in Biorelevant ATCUN/NTS Complexes.Angewandte Chemie (International ed. in English) · 2020Article
- Cu(I) Controls Conformational States in Human Atox1 Metallochaperone: An EPR and Multiscale Simulation Study.The journal of physical chemistry. B · 2020Article
- Article
- X-ray structures of the high-affinity copper transporter Ctr1.Nature communications · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cellular acquisition of copper in eukaryotes is primarily accomplished through the Ctr family of copper transport proteins. In both humans and yeast, methionine-rich "Mets" motifs in the amino-terminal extracellular domain of Ctr1 are thought to be responsible for recruitment of copper at the cell surface. Unlike yeast, mammalian Ctr1 also contains extracellular histidine-rich motifs, although a role for these regions in copper uptake has not been explored in detail. Herein, synthetic model peptides containing the first 14 residues of the extracellular domain of human Ctr1 (MDHSHHMGMSYMDS) have been prepared and evaluated for their apparent binding affinity to both Cu(I) and Cu(II). These studies reveal a high affinity Cu(II) binding site (log K = 11.0 ± 0.3 at pH 7.4) at the amino-terminus of the peptide as well as a high affinity Cu(I) site (log K = 10.2 ± 0.2 at pH 7.4) that utilizes adjacent HH residues along with an additional His or Met ligand. These model studies suggest that the histidine domains may play a direct role in copper acquisition from serum copper-binding proteins and in facilitating the reduction of Cu(II) to the active Ctr1 substrate, Cu(I). We tested this hypothesis by expressing a Ctr1 mutant lacking only extracellular histidine residues in Ctr1-knockout mouse embryonic fibroblasts. Results from live cell studies support the hypothesis that extracellular amino-terminal His residues directly participate in the copper transport function of Ctr1.
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