Hepcidin Revisited, Disulfide Connectivity, Dynamics, and Structure
By J. B. Jordan, L. Poppe, M. Haniu, T. Arvedson, R. Syed, V. Li, H. Kohno, Helen Kim, P. Schnier, T. Harvey and 3 more. 2009
214 citations recorded by the source corpus.
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: Cys1–Cys8, Cys3–Cys6, Cys2–Cys4, and Cys5–Cys7. NMR studies reveal a new model for hepcidin that, at ambient temperatures, interconverts between two different conformations, which could be individually resolved by temperature variation. Using these methods, the solution structure of hepcidin was determined at 325 and 253 K in supercooled water. X-ray analysis of a co-crystal with Fab appeared to stabilize a hepcidin conformation similar to the high temperature NMR structure.
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Citations in the corpus
- Toward the estimation of the absolute quality of individual protein structure models (2010, background): “Figure 1 shows the effect of the normalization on the all-atom potential.”
- Systemic iron homeostasis. (2013, background): “The rest of the molecule is a bent -hairpin crosslinked by highly conserved disulfide bonds (123), with the turn of the hairpin the most variable portion of the molecule.”