Skip to main content
Fig. 3 | Cellular & Molecular Biology Letters

Fig. 3

From: A novel serum spherical lectin from lamprey reveals a more efficient mechanism of immune initiation and regulation in jawless vertebrates

Fig. 3

Comparative analysis of LSSL, hIntL-1, and XEEL. A Structure of the LSSL trimer with two calcium-ion-binding sites oriented with the intelectin-specific domains toward the top of and the fibrinogen-like lobes below the figure. Calcium site with two calcium ions (green) and no water molecules. The other calcium is buried deep in the protein core. B, C Comparison of the structure of lectins from lamprey (wheat), Xenopus (blue), and humans (cyan). The overall structure is shown in B. The Ca2+ binding site 1 and site 2 are shown in C. D Docking of Galβ1-3GlcNAc, Manα1-2Man, and Neu5Ac in the LSSL structure. The calcium ions are shown in green. E Sequence ratio pairs of XEEL and intelectins from humans [hIntL-1 (human intelectin-1) and hIntL-2 (human intelectin-2)] and common model organisms (XCGL-1, XCGL-2, XSL-1, and XSL-2 from X. laevis; mIntL-1 and mIntL-2 from mouse; DrIntL-1 and DrIntL-2 from zebrafish). The corresponding GenBank accession numbers are included in the second column. Residues in the structural calcium site and ligand-binding site are highlighted in blue (LSSL) and orange (hIntL-1/XEEL), respectively

Back to article page