1M4F
Solution Structure of Hepcidin-25
1M4F の概要
エントリーDOI | 10.2210/pdb1m4f/pdb |
関連するPDBエントリー | 1m4e |
NMR情報 | BMRB: 5501 |
分子名称 | Hepcidin (1 entity in total) |
機能のキーワード | strand-loop-strand, beta-sheet, hairpin loop, antimicrobial protein |
細胞内の位置 | Secreted: P81172 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 2802.45 |
構造登録者 | Hunter, H.N.,Fulton, D.B.,Ganz, T.,Vogel, H.J. (登録日: 2002-07-02, 公開日: 2002-11-06, 最終更新日: 2024-10-16) |
主引用文献 | Hunter, H.N.,Fulton, D.B.,Ganz, T.,Vogel, H.J. The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J.Biol.Chem., 277:37597-37603, 2002 Cited by PubMed Abstract: 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. PubMed: 12138110DOI: 10.1074/jbc.M205305200 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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