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Properties of recombinant extracellular N-terminal domain of human high-affinity copper transporter 1 (hNdCTR1) and its interactions with Cu(II) and Ag(I) ionsстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 20 февраля 2024 г.
- Авторы: Orlov Iurii A., Sankova Tatiana P., Skvortsov Alexey N., Klotchenko Sergey A., Sakhenberg Elena I., Mekhova Aleksandra A., Kiseleva Irina V., Ilyechova Ekaterina Yu, Puchkova Ludmila V.
- Журнал: Dalton Transactions
- Том: 52
- Номер: 11
- Год издания: 2023
- Издательство: Royal Society of Chemistry
- Местоположение издательства: United Kingdom
- Первая страница: 3403
- Последняя страница: 3419
- DOI: 10.1039/d2dt04060c
- Аннотация: 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.
- Добавил в систему: Сахенберг Елена Игоревна