An improved structural model of the human iron exporter ferroportin. Insight into the role of pathogenic mutations in hereditary hemochromatosis type 4

• Autorzy: Tortosa V. , Bonaccorsi di Patti M. C. , Brandi V. , Musci G. , Polticelli F.

Identyfikatory

DOI

10.1515/bams-2017-0029

• Języki publikacji: EN

Abstrakty

EN

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 outwardfacing 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.

Słowa kluczowe

EN

ferroportin; iron transport; major facilitator superfamily; molecular modeling

• Wydawca: Uniwersytet Jagielloński - Collegium Medicum ; De Gruyter
• Czasopismo: Bio-Algorithms and Med-Systems
• Rocznik: 2017
• Tom: Vol. 13, no. 4
• Strony: 215--222
• Opis fizyczny: Bibliogr. 34 poz., rys.

Twórcy

autor

Tortosa V.

• Department of Sciences, Roma Tre University, 00146 Rome, Italy

autor

Bonaccorsi di Patti M. C.

• Department of Biochemical Sciences, Sapienza University of Roma, 00185 Rome, Italy

autor

Brandi V.

• Department of Sciences, Roma Tre University, 00146 Rome, Italy

autor

Musci G.

• Department of Biosciences and Territory, University of Molise, 86090 Pesche, Italy

autor

Polticelli F.

• Department of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, 00146 Rome, Italy, Phone: [phone], Fax: [phone]

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