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.
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| Title: | 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. |
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| Authors: | Orlov, Iurii A.1 (AUTHOR), Sankova, Tatiana P.2 (AUTHOR), Skvortsov, Alexey N.2,3 (AUTHOR), Klotchenko, Sergey A.4 (AUTHOR), Sakhenberg, Elena I.5 (AUTHOR), Mekhova, Aleksandra A.1,2 (AUTHOR), Kiseleva, Irina V.6 (AUTHOR), Ilyechova, Ekaterina Yu.1,2,7 (AUTHOR) ilichevaey@itmo.ru, Puchkova, Ludmila V.1,2,7 (AUTHOR) |
| Source: | Dalton Transactions: An International Journal of Inorganic Chemistry. 3/21/2023, Vol. 52 Issue 11, p3403-3419. 17p. |
| Subjects: | Copper, Isothermal titration calorimetry, Silver ions, Extracellular space, Gene expression |
| Abstract: | 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. [ABSTRACT FROM AUTHOR] |
| Copyright of Dalton Transactions: An International Journal of Inorganic Chemistry is the property of Royal Society of Chemistry and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 162412781 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: 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. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Orlov%2C+Iurii+A%2E%22">Orlov, Iurii A.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Sankova%2C+Tatiana+P%2E%22">Sankova, Tatiana P.</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Skvortsov%2C+Alexey+N%2E%22">Skvortsov, Alexey N.</searchLink><relatesTo>2,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Klotchenko%2C+Sergey+A%2E%22">Klotchenko, Sergey A.</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Sakhenberg%2C+Elena+I%2E%22">Sakhenberg, Elena I.</searchLink><relatesTo>5</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Mekhova%2C+Aleksandra+A%2E%22">Mekhova, Aleksandra A.</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kiseleva%2C+Irina+V%2E%22">Kiseleva, Irina V.</searchLink><relatesTo>6</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Ilyechova%2C+Ekaterina+Yu%2E%22">Ilyechova, Ekaterina Yu.</searchLink><relatesTo>1,2,7</relatesTo> (AUTHOR)<i> ilichevaey@itmo.ru</i><br /><searchLink fieldCode="AR" term="%22Puchkova%2C+Ludmila+V%2E%22">Puchkova, Ludmila V.</searchLink><relatesTo>1,2,7</relatesTo> (AUTHOR) – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Dalton+Transactions%3A+An+International+Journal+of+Inorganic+Chemistry%22">Dalton Transactions: An International Journal of Inorganic Chemistry</searchLink>. 3/21/2023, Vol. 52 Issue 11, p3403-3419. 17p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Copper%22">Copper</searchLink><br /><searchLink fieldCode="DE" term="%22Isothermal+titration+calorimetry%22">Isothermal titration calorimetry</searchLink><br /><searchLink fieldCode="DE" term="%22Silver+ions%22">Silver ions</searchLink><br /><searchLink fieldCode="DE" term="%22Extracellular+space%22">Extracellular space</searchLink><br /><searchLink fieldCode="DE" term="%22Gene+expression%22">Gene expression</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: 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. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Dalton Transactions: An International Journal of Inorganic Chemistry is the property of Royal Society of Chemistry and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1039/d2dt04060c Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 17 StartPage: 3403 Subjects: – SubjectFull: Copper Type: general – SubjectFull: Isothermal titration calorimetry Type: general – SubjectFull: Silver ions Type: general – SubjectFull: Extracellular space Type: general – SubjectFull: Gene expression Type: general Titles: – TitleFull: 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. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Orlov, Iurii A. – PersonEntity: Name: NameFull: Sankova, Tatiana P. – PersonEntity: Name: NameFull: Skvortsov, Alexey N. – PersonEntity: Name: NameFull: Klotchenko, Sergey A. – PersonEntity: Name: NameFull: Sakhenberg, Elena I. – PersonEntity: Name: NameFull: Mekhova, Aleksandra A. – PersonEntity: Name: NameFull: Kiseleva, Irina V. – PersonEntity: Name: NameFull: Ilyechova, Ekaterina Yu. – PersonEntity: Name: NameFull: Puchkova, Ludmila V. IsPartOfRelationships: – BibEntity: Dates: – D: 21 M: 03 Text: 3/21/2023 Type: published Y: 2023 Identifiers: – Type: issn-print Value: 14779226 Numbering: – Type: volume Value: 52 – Type: issue Value: 11 Titles: – TitleFull: Dalton Transactions: An International Journal of Inorganic Chemistry Type: main |
| ResultId | 1 |
