title: Molecular architecture of mouse activating NKR-P1 receptors.
abstract: 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.
authors: Institute of Macromolecular Chemistry, v.v.i., Academy of Sciences of the Czech Republic, Heyrovského náměstí 2, 16206 Prague 6, Czech Republic.
authors: Petr
authors: P
authors: Kolenko
authors: Daniel
authors: D
authors: Rozbeský
authors: Ondřej
authors: O
authors: Vaněk
authors: Vladimír
authors: V
authors: Kopecký
authors: Kateřina
authors: K
authors: Hofbauerová
authors: Petr
authors: P
authors: Novák
authors: Petr
authors: P
authors: Pompach
authors: Jindřich
authors: J
authors: Hašek
authors: Tereza
authors: T
authors: Skálová
authors: Karel
authors: K
authors: Bezouška
authors: Jan
authors: J
authors: Dohnálek