Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A structural model of human ferroportin and of its iron binding site.

The FEBS journal - 1 Jun 2014

Bonaccorsi di Patti Maria C, Polticelli Fabio, Cece Giovanna, Cutone Antimo, Felici Franco, Persichini Tiziana, Musci Giovanni

Abstract excerpt

A structural model of human ferroportin has been built using two Escherichia coli proteins belonging to the major facilitator superfamily of transporters. A potential iron binding site was identified in the inward-open conformation of the model, and its relevance was tested through measurement of iron export of HEK293T cells expressing wild-type or mutated ferroportin. Aspartates 39 and 181 were found to be...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cation Transport Proteins
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ferroportin

Share to HEK293 Cells

Share to Hemochromatosis

Share to Ligands

Share to Protein Conformation

Source

Identifiers

PMID: 24767627
DOI: 10.1111/febs.12825

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A structural model of human ferroportin and of its iron binding site.PMID 24767627Read ↗

Structure-function analysis of the human ferroportin iron exporter (SLC40A1): effect of hemochromatosis type 4 disease mutations and identification of critical residues.Semantic proximity Read ↗

Computational Studies of the Dynamics of the Human Iron Exporter Ferroportin: Insight into the Role of Crucial Residues Involved in Pathogenic Mutations in the Transport MechanismSemantic proximity Read ↗

Structural models of the human iron exporter ferroportin in the inward- and outward- open statesSemantic proximity Read ↗

Molecular model of the ferroportin intracellular gate and implications for the human iron transport cycle and hemochromatosis type 4A.Semantic proximity Read ↗

Structure and mechanism of a primate ferroportinSemantic proximity Read ↗

The dual loss and gain of function of the FPN1 iron exporter results in the ferroportin disease phenotype.Semantic proximity Read ↗

The dynamics of hepcidin-ferroportin internalization and consequences of a novel ferroportin disease mutation.Semantic proximity Read ↗

Functional analysis and theoretical modeling of ferroportin reveals clustering of mutations according to phenotype.Semantic proximity Read ↗

A bacterial homologue of the human iron exporter ferroportin.Semantic proximity Read ↗

Structure-function analysis of ferroportin defines the binding site and an alternative mechanism of action of hepcidin.Semantic proximity Read ↗

Structures of ferroportin in complex with its specific inhibitor vamifeportSemantic proximity Read ↗

Impact of D181V and A69T on the function of ferroportin as an iron export pump and hepcidin receptor.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.