TY  - JOUR
AU  - Balaji, GR
AU  - Aguilar, OA
AU  - Tanaka, M
AU  - Shingu-Vazquez, MA
AU  - Fu, Z
AU  - Gully, BS
AU  - Lanier, LL
AU  - Carlyle, JR
AU  - Rossjohn, J
AU  - Berry, R
Y2  - 2020/12/09
Y1  - 2018/11/05
SN  - 2041-1723
UR  - http://hdl.handle.net/11343/253243
AB  - 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.
LA  - English
PB  - NATURE PUBLISHING GROUP
T1  - Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition
DO  - 10.1038/s41467-018-06989-2
IS  - Nature Communications
VL  - 9
IS  - 1
L1  - /bitstream/handle/11343/253243/PMC6218473.pdf?sequence=1&isAllowed=y
ER  -