Structure-function analysis of ferroportin defines the binding site and an alternative mechanism of action of hepcidin

著者: Sharraya Aschemeyer, Bo Qiao, D Stefanova, Erika V. Valore, Albert C. Sek, T Alex Ruwe, Kyle R. Vieth, Grace Jung, Carla Casu, Stefano Rivella, Mika Jormakka, Bryan Mackenzie, Tomas Ganz, Elizabeta Nemeth - Blood 2017 被引用: 326

oocytes expressing wild-type or K8R Fpn, and mature human red blood cells. We conclude that nonclassical FD is caused by Fpn mutations that decrease hepcidin binding or hinder conformational changes required for ubiquitination and endocytosis of Fpn. The newly documented ability of hepcidin and its agonists to occlude iron transport may facilitate the development of broadly effective treatments for hereditary iron overload disorders.