Molecular architecture of mouse activating NKR-P1 receptors |
| |
Authors: | Kolenko Petr Rozbeský Daniel Vaněk Ond?ej Kopecký Vladimír Hofbauerová Kate?ina Novák Petr Pompach Petr Ha?ek Jind?ich Skálová Tereza Bezou?ka Karel Dohnálek Jan |
| |
Institution: | Institute of Macromolecular Chemistry, v.v.i., Academy of Sciences of the Czech Republic, Heyrovského náměstí 2, 16206 Prague 6, Czech Republic. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|