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Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms

Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7906036

Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms

About this item

Full title

Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2020-10, Vol.586 (7831), p.807-811

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The serum level of iron in humans is tightly controlled by the action of the hormone hepcidin on the iron efflux transporter ferroportin. Hepcidin regulates iron absorption and recycling by inducing the internalization and degradation of ferroportin
1
. Aberrant ferroportin activity can lead to diseases of iron overload, such as haemochromato...

Alternative Titles

Full title

Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7906036

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7906036

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/s41586-020-2668-z

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