2KEF

Solution NMR structures of human hepcidin at 325K

2KEF の概要

• エントリーDOI: 10.2210/pdb2kef/pdb
• 分子名称: Hepcidin (1 entity in total)
• 機能のキーワード: hepcidin, antibiotic, antimicrobial, cleavage on pair of basic residues, disease mutation, fungicide, hormone, secreted
• 由来する生物種: Homo sapiens (Human)
• 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

Jordan, J.B.,Poppe, L.,Hainu, M.,Arvedson, T.,Syed, R.,Li, V.,Kohno, H.,Kim, H.,Miranda, L.P.,Cheetham, J.,Sasu, B.J. (登録日: 2009-01-29, 公開日: 2009-06-23, 最終更新日: 2024-10-30)

主引用文献

Jordan, J.B.,Poppe, L.,Haniu, M.,Arvedson, T.,Syed, R.,Li, V.,Kohno, H.,Kim, H.,Schnier, P.D.,Harvey, T.S.,Miranda, L.P.,Cheetham, J.,Sasu, B.J.
Hepcidin revisited, disulfide connectivity, dynamics, and structure.
J.Biol.Chem., 284:24155-24167, 2009

PubMed Abstract: 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 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.

PubMed: 19553669
DOI: 10.1074/jbc.M109.017764

実験手法

SOLUTION NMR