3H0T

Hepcidin-Fab complex

Summary for 3H0T

• Entry DOI: 10.2210/pdb3h0t/pdb
• Descriptor: Fab fragment, Light chain, Fab fragment, Heavy chain, Hepcidin, ... (4 entities in total)
• Functional Keywords: peptide-fab complex, antibiotic, antimicrobial, cleavage on pair of basic residues, disease mutation, disulfide bond, fungicide, hormone, secreted, immune system-antimicrobial protein complex, immune system/antimicrobial protein
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P81172
• Total number of polymer chains: 3
• Total formula weight: 51436.13

Authors

Syed, R.,Li, V. (deposition date: 2009-04-10, release date: 2009-06-23, Last modification date: 2024-11-20)

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

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

Experimental method

X-RAY DIFFRACTION (1.89 Å)