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

Balaji, Gautham R., Aguilar, Oscar A., Tanaka, Miho, Shingu-Vazquez, Miguel A., Fu, Zhihui, Gully, Benjamin S., Lanier, Lewis L., Carlyle, James R., Rossjohn, Jamie and Berry, Richard 2018. Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition. Nature Communications 9 (1) , 4623. 10.1038/s41467-018-06989-2

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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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Publisher: Nature Publishing Group
ISSN: 2041-1723
Date of First Compliant Deposit: 20 November 2018
Date of Acceptance: 9 October 2018
Last Modified: 23 Nov 2018 15:45
URI: http://orca.cf.ac.uk/id/eprint/116952

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