Homo-oligomerization of the Activating Natural Killer Cell Receptor NKp30 Ectodomain Increases Its Binding Affinity for Cellular Ligands
| Autor: | Steffen Beyer, Hannah Berberich, Jessica Hartmann, Joachim Koch, Julia Herrmann, Karen M. Davies |
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| Rok vydání: | 2014 |
| Předmět: |
B7 Antigens
Immunology Immunoblotting chemical and pharmacologic phenomena Biology Ligands Binding Competitive Biochemistry Cell Line Natural killer cell Sf9 Cells medicine Animals Humans Binding site Receptor Molecular Biology Cells Cultured Binding Sites Microscopy Confocal Natural Cytotoxicity Triggering Receptor 3 Innate immune system Cell Membrane Cell Biology Ligand (biochemistry) Cell biology Killer Cells Natural Microscopy Electron HEK293 Cells medicine.anatomical_structure Membrane protein Ectodomain Protein Multimerization Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 289:765-777 |
| ISSN: | 0021-9258 |
| Popis: | The natural cytotoxicity receptors, comprised of three type I membrane proteins NKp30, NKp44, and NKp46, are a unique set of activating proteins expressed mainly on the surface of natural killer (NK) cells. Among these, NKp30 is a major receptor targeting virus-infected cells, malignantly transformed cells, and immature dendritic cells. To date, only few cellular ligands of NKp30 have been discovered, and the molecular details of ligand recognition by NKp30 are poorly understood. Within the current study, we found that the ectodomain of NKp30 forms functional homo-oligomers that mediate high affinity binding to its corresponding cellular ligand B7-H6. Notably, this homo-oligomerization is strongly promoted by the stalk domain of NKp30. Based on these data, we suggest that homo-oligomerization of NKp30 in the plasma membrane of NK cells, which might be favored by IL-2-dependent up-regulation of NKp30 expression, provides a way to improve recognition and lysis of target cells by NK cells. |
| Databáze: | OpenAIRE |
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