Activating killer cell immunoglobulin-like receptor 2DS2 binds to HLA-A*11
Copyright policy )Activating killer cell immunoglobulin-like receptor 2DS2 binds to HLA-A*11
Significance Killer cell immunoglobulin-like receptors (KIRs) function as key recognition elements in innate immunity. Structural information for inhibitory KIRs 2DL2, 2DL1, and 3DL1 in complex with their respective HLA ligands is available, but such data for activating KIRs are lacking. We report here the successful crystallization and solved structure of the activating KIR2DS2 in complex with HLA-A*11:01. The structure clearly explains the role of Tyr45, which has long puzzled KIR researchers because it differentiates KIR2DS2 from all inhibitory KIRs, and is now shown to bind Thr80 of HLA-A*11:01. Using KIR2DS2 tetramers to bind HLA on live cells, we also provide evidence that peptide sequence can affect KIR–HLA binding. Our data thus resolve a long-standing problem in KIR biology.
- National University of Singapore Singapore
- Agency for Science, Technology and Research Singapore
Models, Molecular, Threonine, Protein Conformation, Reverse Transcriptase Polymerase Chain Reaction, Surface Plasmon Resonance, Immunity, Innate, Cell Line, HLA-A11 Antigen, Killer Cells, Natural, Receptors, KIR, X-Ray Diffraction, Mutagenesis, Escherichia coli, Humans, Tyrosine, Crystallization, Fluorescein-5-isothiocyanate
Models, Molecular, Threonine, Protein Conformation, Reverse Transcriptase Polymerase Chain Reaction, Surface Plasmon Resonance, Immunity, Innate, Cell Line, HLA-A11 Antigen, Killer Cells, Natural, Receptors, KIR, X-Ray Diffraction, Mutagenesis, Escherichia coli, Humans, Tyrosine, Crystallization, Fluorescein-5-isothiocyanate
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