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. 2017 Oct 2;8:764. doi: 10.1038/s41467-017-00836-6

Fig. 2.

Fig. 2

Differences in ligand binding domain d1 among the Siglec family. a Sequence alignment of the V-type domain of mammalian CD22 and other Siglecs. Siglec -1, -4, -5, -7, and -8. hCD22 secondary structure elements are represented atop the alignment. Putative N-glycosylation sites N67, N101, N112, and N135 are highlighted in blue boxes. Conserved R120 involved in binding Sia ligands is marked by a red box. b Comparison of available three-dimensional structures of V-type domains from classic Siglecs (including the CD22 structure reported here, Siglec-1 (PDB ID: 1QFP)67 and Siglec-4 (PDB ID: 5LFR)23) and CD33/Siglec-3-related Siglecs (Siglec-5 (PDB ID: 2ZG2)24, Siglec-7 (PDB ID: 1O7S)26, and Siglec-8 (PDB ID: 2N7A)51). Differences in C–C′ (blue), C′–D (red), and strand G (orange) conformations are highlighted. R120 is shown as sticks. c Uniqueness of the CD22 V-type fold compared to other Siglecs is evident from elevated Cα r.m.s.d. values calculated with MOE60. hCD22 human CD22, cCD22 CD22 from Pan troglodites (chimpanzee), bCD22 CD22 from Pan paniscus (bonobo), gCD22 CD22 from Gorilla gorilla (gorilla), oCD22 CD22 from Pongo pygmaeous (orangutan), mCD22 CD22 from Mus musculus (mouse)