Ontology highlight
ABSTRACT:
SUBMITTER: Jordan JB
PROVIDER: S-EPMC2782009 | biostudies-literature | 2009 Sep
REPOSITORIES: biostudies-literature
Jordan John B JB Poppe Leszek L Haniu Mitsuru M Arvedson Tara T Syed Rashid R Li Vivian V Kohno Hiko H Kim Helen H Schnier Paul D PD Harvey Timothy S TS Miranda Les P LP Cheetham Janet J Sasu Barbra J BJ
The Journal of biological chemistry 20090624 36
Hepcidin is a tightly folded 25-residue peptide hormone containing four disulfide bonds, which has been shown to act as the principal regulator of iron homeostasis in vertebrates. We used multiple techniques to demonstrate a disulfide bonding pattern for hepcidin different from that previously published. All techniques confirmed the following disulfide bond connectivity: Cys(1)-Cys(8), Cys(3)-Cys(6), Cys(2)-Cys(4), and Cys(5)-Cys(7). NMR studies reveal a new model for hepcidin that, at ambient t ...[more]