Comprehensive analysis of lectin-glycan interactions reveals determinants of lectin specificity
Fig 1
Lectin-glycan interaction characterization and comparison.
Features for lectin-glycan interactions (A) are derived from Protein-Ligand Interaction Profiler (PLIP) defined interaction counts (B), voxelized representations of the 3D pocket space occupied by the glycan (C), and binding site residues binned by their minimum distance to the glycan (D). Two types of specificity analyses were conducted. For global specificity (E), binding interaction characteristics from each glycan of interest were compared to the background characteristics of all other lectin-glycan interactions, revealing features that were enriched or depleted in association with the presence of the given glycan relative to all other glycans. For fine specificity (F), characteristics were compared among interactions within a subgroup of similar glycans. In panels A-D, the binding interaction between human lung collectin surfactant protein D and a disaccharide fragment (Hep-Kdo) of a bacterial lipopolysaccharide is used to demonstrate the three categories of interaction features (PDB ID: 4E52). Panel C has additional components illustrating featurization of the voxel point cloud via features describing the D2 distribution of pairwise distances between surface points and computed 3D Zernike descriptors (3DZDs), with the original point cloud in red and the reconstructed shape from the 3DZDs in blue. Panels E & F display schematic results of select features defined in panels B-D that were found to be significantly enriched or depleted in the specified interactions. Structures were rendered using PyMol and glycan symbols follow the Symbol Nomenclature for Glycans (SNFG) system.