EPR Spectroscopy Shows that
the Blood Carrier Protein,
Human Serum Albumin, Closely Interacts with the N‑Terminal
Domain of the Copper Transporter, Ctr1
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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