Fig. 4
β-D-Glucan structures facilitate the interactions between NLGP and Dectin-1. a The regression line and equation between concentrations of NLGP and β-1,3-D-Glucan, determined by ELISA (n = 3), as mean ± SD with the R2 value. b β-1,3-D-Glucan quantified within NLGP in a part of whole pie-chart series, where 10% of the first pie chart (Pie 1) is taken as Pie 2 and 10% of Pie 2 is considered as Pie 3. β-1,3-D-Glucan occupied 23.74% of Pie 3, thereby constituting 0.2374% (w/w) of NLGP. c Three abundant short β-D-Glucan structures as flexible small molecules (ligands) for molecular docking. d Ribbon (upper), and surface (middle and lower) representations of the dimeric crystal structure of murine Dectin-1 (CLEC7A) (2BPE from RCSB PDB). Cytosolic ITAM sequences highlighted in black, in the ribbon diagram (upper) (ITAM stands for Immunoreceptor tyrosine-based activation motif). Surface model in the middle represents extents of hydrophobicity at different regions. e Docked β-D-Glucan structures shown in front and back-views of the Dectin-1 dimer (center) (See also Additional file 4). Localized interactions of Glucans and Dectin-1 amino acids are magnified as 3D (views with the macromolecular surface within circles, and views without the macromolecular surface outside circles) and 2D views. Types of chemical bonds participating in interactions are enlisted in legend at bottom right corner