Molecular architecture of mouse activating NKR-P1 receptors.

Research paper by Petr P Kolenko, Daniel D Rozbeský, Ondřej O Vaněk, Vladimír V Kopecký, Kateřina K Hofbauerová, Petr P Novák, Petr P Pompach, Jindřich J Hašek, Tereza T Skálová, Karel K Bezouška, Jan J Dohnálek

Indexed on: 24 May '11Published on: 24 May '11Published in: Journal of Structural Biology


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.