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. 2018 Dec 14;38(6):BSR20181787. doi: 10.1042/BSR20181787

Figure 1. The overlay of wild-type Gal-13 (labeled by green) with the Gal-3 CRD (PDB: 4R9C, labeled by cyan) and Gal-8 N-terminal CRD (PDB: 5GZD, labeled by purple).

Figure 1

The corresponding residues of Gal-13 Arg53, Arg55, and His57 in Gal-3 CRD and Gal-8 N CRD are histidine, asparagine, and arginine, respectively. The three residues in the sugar binding sites of Gal-3 CRD and Gal-8 N CRD are important for binding lactose. In the present study, Gal-13 Arg53, Arg55, and His57 were mutated to the corresponding residues in Gal-3 CRD and Gal-8 N CRD (Table 1). Asp33 could insert into the sugar binding site of another Gal-13 monomer in another asymmetric unit. This aspartate residue was also mutated to glycine.