Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5914801 | Journal of Structural Biology | 2011 | 8 Pages |
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
DLSNKRFT-MSNatural killer cell receptorCTLDITAMCLRKirRMSDDTTDSCEDCPVDFtris(2-carboxyethyl)phosphinevdWReceptor–ligand interactionmolecular replacementdithiothreitolX-ray structureTCEPNK cellFourier-Transform mass spectrometryMass spectrometryimmunoreceptor tyrosine-based activation motifroot mean square deviationVan der WaalsDynamic Light ScatteringPolyvinylidene fluorideDifferential scanning calorimetrykiller-cell immunoglobulin-like receptorC-type lectin receptor
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Authors
Petr Kolenko, Daniel Rozbeský, OndÅej VanÄk, VladimÃr Jr., KateÅina Hofbauerová, Petr Novák, Petr Pompach, JindÅich HaÅ¡ek, Tereza Skálová, Karel BezouÅ¡ka, Jan Dohnálek,