<unk>  exists as a preprohormone (84 amino acids), prohormone (60 amino acids), and hormone (25 amino acids). Twenty- and 22-amino acid metabolites of<unk>  also exist in the urine. Deletion of 5 N-terminal amino acids results in loss of function. The conversion of prohepcidin to<unk>  is mediated by the prohormone convertase furin. This conversion may be regulated by alpha-1 antitrypsin.<unk>  is a tightly folded polypeptide with 32% beta sheet character and a hairpin structure stabilized by 4 disulfide bonds. The structure of<unk>  has been determined through solution NMR. NMR studies showed a new model for<unk> : at ambient temperatures, the protein interconverts between two conformations, which could be individually resolved by temperature variation. The solution structure of<unk>  was determined at 325 K and 253 K in supercooled water. X-ray analysis of a co-crystal with Fab revealed a structure similar to the high-temperature NMR structure.
Hepcidin
Ferritin
Ovoferrin
Beta-2 transferrin
Thyroglobulin
Gamma globulin
Alpha-1 antitrypsin
Toxidrome