Fig. 1

Structures and sequence analysis of Acan-Gal-1. a Schematic diagram showing the domains of Acan-Gal-1 (residues 1–285). b Alignment of amino acid sequences of Acan-Gal-1 from A. cantonensis with that from C. elegans and the secondary structures. The accession number of Ce-Lec-1 sequence available from the current database is: NP_001370038.1. Identical and similar residues are shown in black and gray blocks, respectively. Secondary elements are shown by coil (α-helix) and arrows (green indicates β-sheets of NCRD and blue indicates those of CCRD). The short linker between NCRD and CCRD is indicated by a red line. The conserved motifs HXXXR and WGXEER are indicated by blue boxes. The critical amino acids for recognizing carbohydrate binding are indicated by red stars. c Predicted tertiary structure of Acan-Gal-1, HXXXR motif and WGXEER motif in NCRD and CCRD, respectively