Format:
xii, 135 Seiten
,
Illustrationen, Diagramme
Content:
Hepcidin-25 (Hep-25) plays a crucial role in the control of iron homeostasis. Since the dysfunction of the hepcidin pathway leads to multiple diseases as a result of iron imbalance, hepcidin represents a potential target for the diagnosis and treatment of disorders of iron metabolism. Despite intense research in the last decade targeted at developing a selective immunoassay for iron disorder diagnosis and treatment and better understanding the ferroportin-hepcidin interaction, questions remain. The key to resolving these underlying questions is acquiring exact knowledge of the 3D structure of native Hep-25. Since it was determined that the N-terminus, which is responsible for the bioactivity of Hep-25, contains a small Cu(II)-binding site known as the ATCUN motif, it was assumed that the Hep-25-Cu(II) complex is the native, bioactive form of the hepcidin. This structure has thus far not been elucidated in detail. Owing to the lack of structural information on metal-bound Hep-25, little is known about its possible biological role in ...
Note:
Dissertation Universität Potsdam 2020
Additional Edition:
Erscheint auch als Online-Ausgabe Vranic, Marija 3D Structure of the biomarker hepcidin-25 in its native state Potsdam, 2020
Language:
English
Keywords:
Hochschulschrift
Author information:
Weller, Michael G.
Author information:
Wittmann, Valentin
