title: EPR spectroscopy shows that the blood carrier protein, human serum albumin, closely interacts with the N-terminal domain of the copper transporter, Ctr1.
abstract: Copper is an essential metal whose localization within the cells must be carefully controlled to avoid copper dependent redox cycling. Although most of the key proteins involved in cellular copper transfer have been identified, fundamental questions regarding the copper transfer mechanism have yet to be resolved. One of the blood carrier proteins believed to be involved in copper transfer to the cell is human serum albumin (HSA). However, direct evidence for close interaction between HSA and the extracellular domain of the copper transporter Ctr1 has not yet been found. By utilizing EPR spectroscopy, we show here that HSA closely interacts with the first 14 amino acids of the Ctr1, even without the presence of copper ions.
authors: Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel 5290002.
authors: Yulia
authors: Y
authors: Shenberger
authors: Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel 5290002.
authors: Amit
authors: A
authors: Shimshi
authors: Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel 5290002.
authors: Sharon
authors: S
authors: Ruthstein
mesh_terms: D000595:Amino Acid Sequence; D001692:Biological Transport; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000378:metabolism*; D003300:Copper / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000378:metabolism*
chemical_list: D027682:Cation Transport Proteins; D010446:Peptide Fragments; D012709:Serum Albumin; D003300:Copper