Manganese Binding Properties of Human Calprotectin under Conditions of High and Low Calcium: X‑ray Crystallographic and Advanced Electron Paramagnetic Resonance Spectroscopic Analysis

The antimicrobial protein calprotectin (CP), a hetero-oligomer of the S100 family members S100A8 and S100A9, is the only identified mammalian Mn(II)-sequestering protein. Human CP uses Ca(II) ions to tune its Mn(II) affinity at a biologically unprecedented hexahistidine site that forms at the S100A8...

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Veröffentlicht in:	Journal of the American Chemical Society 2015-03, Vol.137 (8), p.3004-3016
Hauptverfasser:	Gagnon, Derek M, Brophy, Megan Brunjes, Bowman, Sarah E. J, Stich, Troy A, Drennan, Catherine L, Britt, R. David, Nolan, Elizabeth M
Format:	Artikel
Sprache:	eng
Schlagworte:	antimicrobial proteins BASIC BIOLOGICAL SCIENCES binding capacity binding sites calcium Calcium - metabolism Crystallography, X-Ray electron paramagnetic resonance spectroscopy Electron Spin Resonance Spectroscopy histidine Histidine - chemistry Humans Imidazoles - chemistry INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY ions Leukocyte L1 Antigen Complex - chemistry Leukocyte L1 Antigen Complex - genetics Leukocyte L1 Antigen Complex - metabolism ligands manganese Manganese - metabolism Models, Molecular Mutation nitrogen Oligopeptides - chemistry Protein Binding Protein Structure, Secondary Protons sodium spectral analysis stable isotopes X-ray diffraction
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