ArticleCell biochemistry and biophysics2012
An all-atom model of the structure of human copper transporter 1.
Article in Cell biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 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
- Human CTR1 Through the Ages: Milestones and Emerging Roles in Disease and Therapy.Biomolecules · 2025Review
- Elevated intracellular copper induces CTR1 monomerization and prevents copper uptake.Nature communications · 2025Article
- Copper Homeostasis in the Model OrganismCells · 2024Review
- Endocytosis of nutrient transporters in fungi: The ART of connecting signaling and trafficking.Computational and structural biotechnology journal · 2021Review
- Structural and Functional Diversity Among the Members of CTR, the Membrane Copper Transporter Family.The Journal of membrane biology · 2020Review
- Copper trafficking in eukaryotic systems: current knowledge from experimental and computational efforts.Current opinion in structural biology · 2019Review
- Unraveling the Impact of Cysteine-to-Serine Mutations on the Structural and Functional Properties of Cu(I)-Binding Proteins.International journal of molecular sciences · 2019Article
- Article
- Copper transporters and copper chaperones: roles in cardiovascular physiology and disease.American journal of physiology. Cell physiology · 2018Review
- Pilot Study ofMolecules (Basel, Switzerland) · 2018Article
- Pilot Study ofScientific reports · 2017Article
- Copper trafficking to the secretory pathway.Metallomics : integrated biometal science · 2016Review
- Copper transporters and chaperones CTR1, CTR2, ATOX1, and CCS as determinants of cisplatin sensitivity.Metallomics : integrated biometal science · 2016Article
- pH-regulated metal-ligand switching in the HM loop of ATP7A: a new paradigm for metal transfer chemistry.Metallomics : integrated biometal science · 2016Article
- The C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1.Biophysical journal · 2016Article
- How Mammalian Cells Acquire Copper: An Essential but Potentially Toxic Metal.Biophysical journal · 2016Review
- The copper transporter 1 (CTR1) is required to maintain the stability of copper transporter 2 (CTR2).Metallomics : integrated biometal science · 2015Article
- EGCG Enhances Cisplatin Sensitivity by Regulating Expression of the Copper and Cisplatin Influx Transporter CTR1 in Ovary Cancer.PloS one · 2015Article
- Lysosome-related organelles as mediators of metal homeostasis.The Journal of biological chemistry · 2014Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Human copper transporter 1 (hCTR1) is the major high affinity copper influx transporter in mammalian cells that also mediates uptake of the cancer chemotherapeutic agent cisplatin. A low resolution structure of hCTR1 determined by cryoelectron microscopy was recently published. Several protein structure simulation techniques were used to create an all-atom model of this important transporter using the low resolution structure as a starting point. The all-atom model provides new insights into the roles of specific residues of the N-terminal extracellular domain, the intracellular loop, and C-terminal region in metal ion transport. In particular, the model demonstrates that the central region of the pore contains four sets of methionine triads in the intramembranous region. The structure confirms that two triads of methionine residues delineate the intramembranous region of the transporter, and further identifies two additional methionine triads that are located in the extracellular N-terminal part of the transporter. Together, the four triads create a structure that promotes stepwise transport of metal ions into and then through the intramembranous channel of the transporter via transient thioether bonds to methionine residues. Putative copper-binding sites in the hCTR1 trimer were identified by a program developed by us for prediction of metal-binding sites. These sites correspond well with the known effects of mutations on the ability of the protein to transport copper and cisplatin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.