Fig. 1: The crystal structure of LGALS-11.

a Structure-based sequence alignment of LGALS-11 natural isoforms. Conserved residues are indicated by white letters with black background, the dissimilar amino acids are indicated by black letters on a white background. The dimer interface is indicated by the black triangles (residue 9 L/Q). An amino acid difference in the putative integrin-binding site is denoted by the grey triangle (residue 124 D/V). Carbohydrate-recognising residues are indicated by blue asterisks. The secondary structures are indicated as beta (β) sheets with horizontal black arrows, turns with TT letters and helices with squiggles. b The crystal structure of LGALS-11, and residues involved in cell attachment. The dimer interface between monomers at residues L9 and S11 of the S1 β-strand via hydrogen bonds in a ball-and-stick representation; β-strands are labelled as S1–S6 and F1–F5 in both monomers (i). Predicted cell attachment residues (L123, D124, V125, R126, G127 and D128) of LGALS-11 in a ball-and-stick representation within the rectangle (red dashed line) (ii). c Residues in LGALS-11 are involved in glycan recognition. The residues R53, N64 and E74 of LGALS-11 make direct contact with β-D-galactose via hydrogen bonding (green dashes), and V62 and W71 make non-bonded contact. Image produced using PDBsum server (https://www.ebi.ac.uk/pdbsum/).