Molecular architecture of mouse activating NKR-P1 receptors

• Published in: Journal of structural biology 2011-09, Vol.175 (3), p.434-441
• Main Authors: Kolenko, Petr, Rozbeský, Daniel, Vaněk, Ondřej, Kopecký, Vladimír, Hofbauerová, Kateřina, Novák, Petr, Pompach, Petr, Hašek, Jindřich, Skálová, Tereza, Bezouška, Karel, Dohnálek, Jan
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; C-type lectin-like receptor; Killer Cells, Natural - metabolism; Mice; Molecular Sequence Data; NK cell; NK Cell Lectin-Like Receptor Subfamily B - chemistry; NK Cell Lectin-Like Receptor Subfamily B - metabolism; Protein Structure, Secondary; Receptor–ligand interaction; Spectrum Analysis, Raman; X-Ray Diffraction; X-ray structure
• ISSN: 1047-8477; 1095-8657
• DOI: 10.1016/j.jsb.2011.05.001

Receptors belonging to NKR-P1 family and their specific Clr ligands form an alternative missing self recognition system critical in immunity against tumors and viruses, elimination of tumor cells subjected to genotoxic stress, activation of T cell dependent immune response, and hypertension. The three-dimensional structure of the extracellular domain of the mouse natural killer (NK) cell receptor mNKR-P1Aex has been determined by X-ray diffraction. The core of the C-type lectin domain (CTLD) is homologous to the other CTLD receptors whereas one quarter of the domain forms an extended loop interacting tightly with a neighboring loop in the crystal. This domain swapping mechanism results in a compact interaction interface. A second dimerization interface resembles the known arrangement of other CTLD NK receptors. A functional dimeric form of the receptor is suggested, with the loop, evolutionarily conserved within this family, proposed to participate in interactions with ligands.