TY - JOUR
T1 - Crystallization and preliminary crystallographic characterization of the extracellular Ig-like domain of human natural killer cell activating receptor NKp44
AU - Cantoni, Claudia
AU - Ponassi, Marco
AU - Biassoni, Roberto
AU - Conte, Romana
AU - Spallarossa, Andrea
AU - Moretta, Alessandro
AU - Moretta, Lorenzo
AU - Bolognesi, Martino
AU - Bordo, Domenico
PY - 2002/10/1
Y1 - 2002/10/1
N2 - The cytolytic activity of human natural killer (NK) cells is regulated by fine balancing between activating and inhibitory signals related to distinct families of inhibitory and triggering receptor molecules. The recent identification of NKp44, a triggering receptor selectively expressed by activated NK cells and playing an important role in the natural cytotoxicity of these cells, opens the way to the characterization of the mechanisms involved in NKp44-mediated NK-cell activation on a structural basis. For this purpose, the NKp44 extracellular Ig-like domain was cloned, overexpressed, refolded and crystallized. Diffraction intensities were collected to a resolution limit of 2.2 Å on a synchrotron source. NKp44 extracellular Ig-like domain crystals belong to the hexagonal space group P6222 (or P6422), with unit-cell parameters a = b = 60.4, c = 197.2 Å, γ = 120°. Evaluation of the crystal packing parameter suggests the presence of one molecule (13.8 kDa) per asymmetric unit, with a solvent volume of 67%.
AB - The cytolytic activity of human natural killer (NK) cells is regulated by fine balancing between activating and inhibitory signals related to distinct families of inhibitory and triggering receptor molecules. The recent identification of NKp44, a triggering receptor selectively expressed by activated NK cells and playing an important role in the natural cytotoxicity of these cells, opens the way to the characterization of the mechanisms involved in NKp44-mediated NK-cell activation on a structural basis. For this purpose, the NKp44 extracellular Ig-like domain was cloned, overexpressed, refolded and crystallized. Diffraction intensities were collected to a resolution limit of 2.2 Å on a synchrotron source. NKp44 extracellular Ig-like domain crystals belong to the hexagonal space group P6222 (or P6422), with unit-cell parameters a = b = 60.4, c = 197.2 Å, γ = 120°. Evaluation of the crystal packing parameter suggests the presence of one molecule (13.8 kDa) per asymmetric unit, with a solvent volume of 67%.
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U2 - 10.1107/S0907444902012325
DO - 10.1107/S0907444902012325
M3 - Article
C2 - 12351833
AN - SCOPUS:0036795405
VL - 58
SP - 1843
EP - 1845
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
SN - 0907-4449
IS - 10 I
ER -