Structural highlights
Function[KLRBA_MOUSE] Plays a stimulatory role on natural killer (NK) cell cytotoxicity.[1] Publication Abstract from PubMedReceptors 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. Molecular architecture of mouse activating NKR-P1 receptors.,Kolenko P, Rozbesky D, Vanek O, Kopecky V Jr, Hofbauerova K, Novak P, Pompach P, Hasek J, Skalova T, Bezouska K, Dohnalek J J Struct Biol. 2011 Sep;175(3):434-41. doi: 10.1016/j.jsb.2011.05.001. Epub 2011 , May 12. PMID:21600988[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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