Fig. 4: The structure of the NKR-P1:LLT1 complex shows two distinct binding modes. | Nature Communications

Fig. 4: The structure of the NKR-P1:LLT1 complex shows two distinct binding modes.

From: Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse

Fig. 4: The structure of the NKR-P1:LLT1 complex shows two distinct binding modes.The alternative text for this image may have been generated using AI.

a The overall organization of the complex crystal structure. The LLT1 dimer (green/lemon) contacts the NKR-P1 dimer, formed by the blue and cyan monomers. The second blue-cyan NKR-P1 dimer is related to the first by crystal symmetry. The cyan NKR-P1 monomer interacts with LLT1 in the primary interaction mode, whereas the blue NKR-P1 monomer engages LLT1 using the secondary interaction interface. A black asterisk marks the mutual accessory contact of NKR-P1 bound in primary and secondary mode. Additionally, the asymmetric unit of the crystal contains another NKR-P1 dimer (pink/magenta) lacking contact with LLT1. b Overall comparison of the structure of dimeric KACL (purple) in complex with two NKp65 monomers (red; https://doi.org/10.2210/pdb4IOP/pdb) and the structure of the LLT1 dimer (green/lemon) with the two interacting NKR-P1 molecules in the primary (cyan, left side) and secondary (blue, right side) binding modes. Comparison with only the primary or secondary NKR-P1:LLT1 interaction modes is highlighted in the lower section (both in a side view, using 90° y-axis rotation). c, d NKR-P1:LLT1 primary and secondary interaction interfaces. Contact residues within 5 Å distance are colored in yellow. Amino acids forming the four strongest contacts are highlighted in red for the primary or magenta for the secondary mode.

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