Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition
AuthorBalaji, GR; Aguilar, OA; Tanaka, M; Shingu-Vazquez, MA; Fu, Z; Gully, BS; Lanier, LL; Carlyle, JR; Rossjohn, J; Berry, R
Source TitleNature Communications
PublisherNATURE PUBLISHING GROUP
University of Melbourne Author/sRossjohn, Jamie
AffiliationMicrobiology and Immunology
Document TypeJournal Article
CitationsBalaji, G. R., Aguilar, O. A., Tanaka, M., Shingu-Vazquez, M. A., Fu, Z., Gully, B. S., Lanier, L. L., Carlyle, J. R., Rossjohn, J. & Berry, R. (2018). Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition. NATURE COMMUNICATIONS, 9 (1), https://doi.org/10.1038/s41467-018-06989-2.
Access StatusOpen Access
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.
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