Mutational Analysis of C-Lobe Ligands of Human Serum Transferrin: Insights into the Mechanism of Iron Release

Each homologous lobe of human serum transferrin (hTF) has one Fe3+ ion bound by an aspartic acid, a histidine, two tyrosine residues, and two oxygens from the synergistic anion, carbonate. Extensive characterization of these ligands in the N-terminal lobe has been carried out. Despite sharing the sa...

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Veröffentlicht in:	Biochemistry (Easton) 2005-06, Vol.44 (22), p.8013-8021
Hauptverfasser:	Mason, Anne B, Halbrooks, Peter J, James, Nicholas G, Connolly, Susan A, Larouche, Julia R, Smith, Valerie C, MacGillivray, Ross T. A, Chasteen, N. Dennis
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding, Competitive - genetics Cell Adhesion - genetics Cell Line Cricetinae Electron Spin Resonance Spectroscopy HeLa Cells Humans Hydrogen-Ion Concentration Iron - metabolism Kinetics Ligands Mutagenesis, Site-Directed Peptide Fragments - biosynthesis Peptide Fragments - genetics Peptide Fragments - isolation & purification Peptide Fragments - metabolism Protein Conformation Receptors, Transferrin - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Spectrophotometry, Ultraviolet Transferrin - biosynthesis Transferrin - chemistry Transferrin - genetics Transferrin - metabolism
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