6E7D

Structure of the inhibitory NKR-P1B receptor bound to the host-encoded ligand, Clr-b

Summary for 6E7D

• Entry DOI: 10.2210/pdb6e7d/pdb
• Descriptor: C-type lectin domain family 2 member D, Killer cell lectin-like receptor subfamily B member 1B allele B, SULFATE ION, ... (5 entities in total)
• Functional Keywords: natural killer cell receptor, c-type lectin related ligand, immune complex, innate immunity, immune system
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 24
• Total formula weight: 363900.76

Authors

Balaji, G.R.,Rossjohn, J.,Berry, R. (deposition date: 2018-07-26, release date: 2018-10-24, Last modification date: 2024-10-30)

Primary citation

Balaji, 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.
Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition.
Nat Commun, 9:4623-4623, 2018

PubMed 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.

PubMed: 30397201
DOI: 10.1038/s41467-018-06989-2

Experimental method

X-RAY DIFFRACTION (2.9 Å)