Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition

Gautham R. Balaji, Oscar A. Aguilar, Miho Tanaka, Miguel A. Shingu-Vazquez, Zhihui Fu, Benjamin S. Gully, Lewis L. Lanier, James R. Carlyle (), Jamie Rossjohn () and Richard Berry ()
Additional contact information
Gautham R. Balaji: Monash University
Oscar A. Aguilar: University of Toronto
Miho Tanaka: University of Toronto
Miguel A. Shingu-Vazquez: Monash University
Zhihui Fu: Monash University
Benjamin S. Gully: Monash University
Lewis L. Lanier: University of California
James R. Carlyle: University of Toronto
Jamie Rossjohn: Monash University
Richard Berry: Monash University

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract The interaction between natural killer (NK) cell inhibitory receptors and their cognate ligands constitutes a key mechanism by which healthy tissues are protected from NK cell-mediated lysis. However, self-ligand recognition remains poorly understood within the prototypical NKR-P1 receptor family. Here we report the structure of the inhibitory NKR-P1B receptor bound to its cognate host ligand, Clr-b. NKR-P1B and Clr-b interact via a head-to-head docking mode through an interface that includes a large array of polar interactions. NKR-P1B:Clr-b recognition is extremely sensitive to mutations at the heterodimeric interface, with most mutations severely impacting both Clr-b binding and NKR-P1B receptor function to implicate a low affinity interaction. Within the structure, two NKR-P1B:Clr-b complexes are cross-linked by a non-classic NKR-P1B homodimer, and the disruption of homodimer formation abrogates Clr-b recognition. These data provide an insight into a fundamental missing-self recognition system and suggest an avidity-based mechanism underpins NKR-P1B receptor function.

Date: 2018
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DOI: 10.1038/s41467-018-06989-2

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