2KEF
Solution NMR structures of human hepcidin at 325K
Summary for 2KEF
| Entry DOI | 10.2210/pdb2kef/pdb |
| Descriptor | Hepcidin (1 entity in total) |
| Functional Keywords | hepcidin, antibiotic, antimicrobial, cleavage on pair of basic residues, disease mutation, fungicide, hormone, secreted |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted: P81172 |
| Total number of polymer chains | 1 |
| Total formula weight | 2802.45 |
| Authors | 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. (deposition date: 2009-01-29, release date: 2009-06-23, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 19553669DOI: 10.1074/jbc.M109.017764 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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