Unknown

Dataset Information

0

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


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.

SUBMITTER: Balaji GR 

PROVIDER: S-EPMC6218473 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Balaji Gautham R GR   Aguilar Oscar A OA   Tanaka Miho M   Shingu-Vazquez Miguel A MA   Fu Zhihui Z   Gully Benjamin S BS   Lanier Lewis L LL   Carlyle James R JR   Rossjohn Jamie J   Berry Richard R  

Nature communications 20181105 1


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  ...[more]

Similar Datasets

| S-EPMC373496 | biostudies-literature
| S-EPMC4041007 | biostudies-literature
2022-10-12 | GSE214867 | GEO
| S-EPMC6738865 | biostudies-literature
2010-03-18 | GSE20935 | GEO
| S-EPMC6738858 | biostudies-literature
2010-03-18 | E-GEOD-20935 | biostudies-arrayexpress
| S-EPMC4961179 | biostudies-literature
| S-EPMC6828740 | biostudies-literature
| S-EPMC3030123 | biostudies-literature