Reconstruction of a helical trimer by the second transmembrane domain of human copper transporter 2 in micelles and the binding of the trimer to silver-Reference-Cited by-同舟云学术

Reconstruction of a helical trimer by the second transmembrane domain of human copper transporter 2 in micelles and the binding of the trimer to silver

Published:2016 Issue:6 Volume:6 Page:4335-4342
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Dong Zhe¹²³⁴,Guan Liping¹²³⁴,Wang Chunyu¹²³⁴,Xu Haoran⁵⁶²³⁴,Li Zhengqiang⁵⁶²³⁴,Li Fei¹²³⁴

Affiliation:

1. State Key Laboratory of Supramolecular Structure and Materials

2. Jilin University

3. Changchun 130012

4. P. R. China

5. Key Laboratory for Molecular Enzymology & Engineering

6. The Ministry of Education

Abstract

The second transmembrane domain of human copper transporter 2 (hCtr2-TMD2) forms a trimer with a weaker intermolecular interaction and a lower affinity for Ag(I) than hCtr1-TMD2 trimer.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/RA/C5RA24889B

Reference39 articles.

1. Biochemical Characterization of the Human Copper Transporter Ctr1

2. Biochemical and Genetic Analyses of Yeast and Human High Affinity Copper Transporters Suggest a Conserved Mechanism for Copper Uptake

3. The Mechanism of Copper Uptake Mediated by Human CTR1

4. Human copper transporter 2 is localized in late endosomes and lysosomes and facilitates cellular copper uptake

5. Ctr2 is partially localized to the plasma membrane and stimulates copper uptake in COS-7 cells

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