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Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn 2+ uptake into the Golg...

Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn 2+ uptake into the Golg...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_37553324

Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn 2+ uptake into the Golgi apparatus

About this item

Full title

Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn 2+ uptake into the Golgi apparatus

Publisher

England

Journal title

Nature communications, 2023-08, Vol.14 (1), p.4770

Language

English

Formats

Publication information

Publisher

England

More information

Scope and Contents

Contents

Zinc ions (Zn
) are vital to most cells, with the intracellular concentrations of Zn
being tightly regulated by multiple zinc transporters located at the plasma and organelle membranes. We herein present the 2.2-3.1 Å-resolution cryo-EM structures of a Golgi-localized human Zn
/H
antiporter ZnT7 (hZnT7) in Zn
-bound and unbound forms...

Alternative Titles

Full title

Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn 2+ uptake into the Golgi apparatus

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmed_primary_37553324

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_37553324

Other Identifiers

E-ISSN

2041-1723

DOI

10.1038/s41467-023-40521-5

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