Fig. 1: Galectin-3 structure, sequence analysis and lipopolysaccharide (LPS) assay.
From: Liquid-liquid phase separation and extracellular multivalent interactions in the tale of galectin-3
a, b Intermolecular and (c) intramolecular galectin-3 interactions identified in a previous study. d A galectin-3 monomer: the structured carbohydrate recognition domain is represented by the solved crystal structure (PDB code, 2NMO), with the (non-canonical) N-terminal domain (NTD)-interaction face (with five β-strands) colored blue and the (canonical) sugar binding face (with six β-strands) colored green. Sugar-specific binding sites are indicated with yellow arrows. e–g Sequence analyses: (e) level of structural disorder (using PONDR79), (f) similarity to prion-like proteins (using PLAAC)53, (g) propensity to form π–π interactions54. h, i Turbidity (O.D600nm) of LPS–galectin-3 samples measured at different protein and LPS concentrations. j Photograph of the CRD-only sample under the maximum turbidity conditions in panel i. k A schematic illustration of the main question of this study: what drives monomeric galectin-3 to agglutinate?.
