Fig. 2: Structural characterization of the galectin-1/CXCL4 complex.
From: Chemokines modulate glycan binding and the immunoregulatory activity of galectins
a Overlay of 1H-15N HSQC spectra of 15N-labeled galectin-1 free (black trace) and bound to CXCL4 (light orange trace). b Histogram plot of CSPs observed for each galectin-1 resonance upon interaction to CXCL4. The dashed line represents 1σ from the average CSP, thereby defining the threshold selection for the most affected residues. Light orange bars correspond to CSP above the threshold. Arrows are pointing toward residue showing intensity decrease upon interaction to CXCL4 (Supplementary Fig. 3). Galectin-1 secondary structures are depicted above the plot. c Chemical shift perturbation mapping onto galectin-1 monomer structure which is shown as a semitransparent solvent-accessible surface with a ribbon model displayed below the surface. Residues presenting CSPs above the threshold (defined in b) are colored in light orange. Main ß-strands affected are labeled. Two galectin-1 orientations are presented: (i) the galectin-1 edge view, opposite to the dimer interface, and (ii) the CBS view with the CBS boundaries plotted in dotted lines. d The structural model of the galectin-1/CXCL4 complex. Galectin-1 is shown as grey ribbon whereas CXCL4 is colored yellow. Galectin-1 residues found at the interface of the complex and presenting CSPs above the threshold (defined in b) are colored in light orange.
