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Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2

Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_6afe0189ea234123a9fa4de9856c2bd5

Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2

About this item

Full title

Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2024-04, Vol.15 (1), p.3616-3616, Article 3616

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

SLC26A2 is a vital solute carrier responsible for transporting essential nutritional ions, including sulfate, within the human body. Pathogenic mutations within SLC26A2 give rise to a spectrum of human diseases, ranging from lethal to mild symptoms. The molecular details regarding the versatile substrate-transporter interactions and the impact of p...

Alternative Titles

Full title

Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_6afe0189ea234123a9fa4de9856c2bd5

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_6afe0189ea234123a9fa4de9856c2bd5

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-024-48028-3

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