An improved structural model of the human iron exporter ferroportin. Insight into the role of pathogenic mutations in hereditary hemochromatosis type 4
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Valentina Tortosa
Abstract
Ferroportin (Fpn) is a membrane protein representing the major cellular iron exporter, essential for metal translocation from cells into plasma. Despite its pivotal role in human iron homeostasis, many questions on Fpn structure and biology remain unanswered. In this work, we present two novel and more reliable structural models of human Fpn (hFpn; inward-facing and outward-facing conformations) obtained using as templates the recently solved crystal structures of a bacterial homologue of hFpn, Bdellovibrio bacteriovorus Fpn. In the absence of an experimentally solved structure of hFpn, the structural predictions described here allow to analyze the role of pathogenic mutations in the Fpn-linked hereditary hemochromatosis disease and represent a valuable alternative for reliable structure-based functional studies on this human iron exporter.
Author contributions: The authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.
Research funding: None declared.
Employment or leadership: None declared.
Honorarium: None declared.
Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.
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Supplemental Material:
The online version of this article offers supplementary material (https://doi.org/10.1515/bams-2017-0029).
©2017 Walter de Gruyter GmbH, Berlin/Boston
Artikel in diesem Heft
- Frontmatter
- Research Articles
- Mechanism of ligand binding – PDZ domain taken as example
- Chain-chain complexation and heme binding in haemoglobin with respect to the hydrophobic core structure
- Modified S-transform as a tool to identify secondary structure elements in RNA
- Electronic health record for elderly patients
- Evaluation of lexicon- and syntax-based negation detection algorithms using clinical text data
- Short Communication
- An improved structural model of the human iron exporter ferroportin. Insight into the role of pathogenic mutations in hereditary hemochromatosis type 4
Artikel in diesem Heft
- Frontmatter
- Research Articles
- Mechanism of ligand binding – PDZ domain taken as example
- Chain-chain complexation and heme binding in haemoglobin with respect to the hydrophobic core structure
- Modified S-transform as a tool to identify secondary structure elements in RNA
- Electronic health record for elderly patients
- Evaluation of lexicon- and syntax-based negation detection algorithms using clinical text data
- Short Communication
- An improved structural model of the human iron exporter ferroportin. Insight into the role of pathogenic mutations in hereditary hemochromatosis type 4
