Fig. 2: The structure of human NKR-P1 shows a unique dimerization interface. | Nature Communications

Fig. 2: The structure of human NKR-P1 shows a unique dimerization interface.

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

Fig. 2

a Ribbon diagram of the NKR-P1 CTLD. Secondary structure elements are labeled in different colors: helix α1 is red, helix α2 is yellow, and β-strands and loops are cyan. b Comparison between NKR-P1 dimers formed by the glycosylated (cyan), deglycosylated free (green), and LLT1-bound (blue) forms of NKR-P1. c Comparison between helices α1- and α2-centered dimerization of murine dectin-1 (https://doi.org/10.2210/pdb2CL8/pdb, magenta) and human LLT1 (https://doi.org/10.2210/pdb4QKI/pdb, green), respectively; helices α1 and α2 are shown in red and yellow. Structural alignments of dectin-1 and NKR-P1 homodimers and LLT1 and NKR-P1 homodimers, prepared by aligning only one monomer from each dimer, are shown on the right-hand side. Although the CTLD fold is conserved in each pair of the aligned monomers, the helix α1- and helix α2-centered dimers show inverse arrangement.

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