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NKG2D is a potent activating receptor on natural killer cells, T cells, and macrophages. Mouse NKG2D interacts with two cell surface ligands related to class I MHC molecules: RAE1 and H60. We used soluble versions of NKG2D, RAE1, and H60 to characterize their interactions. RAE1 and H60 each bind NKG2D with nanomolar affinities, indicating tighter binding than most cell surface immune interactions, but NKG2D binds to H60 with approximately 25-fold higher affinity than to RAE1. RAE1 and H60 compete directly for occupancy of NKG2D, and, thus, NKG2D can be occupied by only one ligand at a time. The NKG2D-H60 interaction is more temperature dependent and makes greater use of electrostatic interactions than the NKG2D-RAE1 interaction. The distinct thermodynamic profiles provide insights into the different molecular mechanisms of the binding interactions.

Type

Journal article

Journal

Immunity

Publication Date

08/2001

Volume

15

Pages

201 - 211

Keywords

Animals, Binding, Competitive, Histocompatibility Antigens Class I, Killer Cells, Natural, Membrane Proteins, Mice, Minor Histocompatibility Antigens, NK Cell Lectin-Like Receptor Subfamily K, Protein Binding, Receptors, Immunologic, Receptors, Natural Killer Cell, Recombinant Proteins, Static Electricity, Thermodynamics