1m4e
From Proteopedia
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Solution Structure of Hepcidin-20
Contents |
Overview
The antibacterial and antifungal peptide hepcidin (LEAP-1) is expressed in, the liver. This circulating peptide has recently been found to also act as, a signaling molecule in iron metabolism. As such, it plays an important, role in hereditary hemochromatosis, a serious iron overload disease. In, this study, we report the solution structures of the hepcidin-20 and -25, amino acid peptides determined by standard two-dimensional (1)H NMR, spectroscopy. These small cysteine-rich peptides form a distorted, beta-sheet with an unusual vicinal disulfide bridge found at the turn of, the hairpin, which is probably of functional significance. Both peptides, exhibit an overall amphipathic structure with six of the eight Cys, involved in maintaining interstrand connectivity. Hepcidin-25 assumes, major and minor conformations centered about the Pro residue near the, N-terminal end. Further NMR diffusion studies indicate that hepcidin-20, exists as a monomer in solution, whereas hepcidin-25 readily aggregates, a, property that may contribute to the different activities of the two, peptides. The nuclear Overhauser enhancement spectroscopy spectra of the, hepcidin-25 aggregates indicate an interface for peptide interactions that, again involves the first five residues from the N-terminal end.
Disease
Known diseases associated with this structure: Hemochromatosis, juvenile OMIM:[606464], Hemochromatosis, juvenile, digenic OMIM:[606464]
About this Structure
1M4E is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis., Hunter HN, Fulton DB, Ganz T, Vogel HJ, J Biol Chem. 2002 Oct 4;277(40):37597-603. Epub 2002 Jul 22. PMID:12138110
Page seeded by OCA on Mon Nov 12 18:07:09 2007
