Properties of recombinant extracellular N-terminal domain of human high-affinity copper transporter 1 (hNdCTR1) and its interactions with Cu(II) and Ag(I) ions
High-affinity copper transporter 1 (CTR1) is a key link in the transfer of copper (Cu) from the extracellular environment to the cell. Violation in the control system of its expression, or mutations in this gene, cause a global copper imbalance. However, the mechanism of copper transfer via CTR1 remains unclear. It has been shown that transformed bacteria synthesizing the fused GB1-NdCTR become resistant to toxic silver ions. According to UV-Vis spectrophotometry and isothermal titration calorimetry, electrophoretically pure GB1-NdCTR specifically and reversibly binds copper and silver ions, and binding is associated with aggregation. Purified NdCTR1 forms SDS-resistant oligomers. The link between nontrivial properties of NdCTR1 and copper import mechanism from extracellular space, as well as potential chelating properties of NdCTR1, are discussed.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:52 |
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| Enthalten in: |
Dalton transactions (Cambridge, England : 2003) - 52(2023), 11 vom: 14. März, Seite 3403-3419 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Orlov, Iurii A [VerfasserIn] |
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| Links: |
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| Themen: |
3M4G523W1G |
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| Anmerkungen: |
Date Completed 15.03.2023 Date Revised 15.03.2023 published: Electronic Citation Status MEDLINE |
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| doi: |
10.1039/d2dt04060c |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM353216100 |
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| 245 | 1 | 0 | |a Properties of recombinant extracellular N-terminal domain of human high-affinity copper transporter 1 (hNdCTR1) and its interactions with Cu(II) and Ag(I) ions |
| 264 | 1 | |c 2023 | |
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| 500 | |a Date Revised 15.03.2023 | ||
| 500 | |a published: Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a High-affinity copper transporter 1 (CTR1) is a key link in the transfer of copper (Cu) from the extracellular environment to the cell. Violation in the control system of its expression, or mutations in this gene, cause a global copper imbalance. However, the mechanism of copper transfer via CTR1 remains unclear. It has been shown that transformed bacteria synthesizing the fused GB1-NdCTR become resistant to toxic silver ions. According to UV-Vis spectrophotometry and isothermal titration calorimetry, electrophoretically pure GB1-NdCTR specifically and reversibly binds copper and silver ions, and binding is associated with aggregation. Purified NdCTR1 forms SDS-resistant oligomers. The link between nontrivial properties of NdCTR1 and copper import mechanism from extracellular space, as well as potential chelating properties of NdCTR1, are discussed | ||
| 650 | 4 | |a Journal Article | |
| 650 | 7 | |a Copper |2 NLM | |
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| 650 | 7 | |a Copper Transporter 1 |2 NLM | |
| 650 | 7 | |a Silver |2 NLM | |
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| 700 | 1 | |a Sankova, Tatiana P |e verfasserin |4 aut | |
| 700 | 1 | |a Skvortsov, Alexey N |e verfasserin |4 aut | |
| 700 | 1 | |a Klotchenko, Sergey A |e verfasserin |4 aut | |
| 700 | 1 | |a Sakhenberg, Elena I |e verfasserin |4 aut | |
| 700 | 1 | |a Mekhova, Aleksandra A |e verfasserin |4 aut | |
| 700 | 1 | |a Kiseleva, Irina V |e verfasserin |4 aut | |
| 700 | 1 | |a Ilyechova, Ekaterina Yu |e verfasserin |4 aut | |
| 700 | 1 | |a Puchkova, Ludmila V |e verfasserin |4 aut | |
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