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.

Institute of Macromolecular Chemistry v v i Academy of Sciences of the Czech Republic Heyrovského náměstí 2 16206 Prague 6 Czech Republic

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Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse

Production of recombinant soluble dimeric C-type lectin-like receptors of rat natural killer cells

Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells

A Hybrid Hamiltonian for the Accelerated Sampling along Experimental Restraints

Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states

Nkrp1 family, from lectins to protein interacting molecules

Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution