XB-IMG-148720
Xenbase Image ID: 148720
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Figure 2. Sequence alignment of malectin proteins in animals. Malectin proteins are composed of an N-terminal signal peptide (SP, AA
1-26), a C-terminal transmembrane helix (TM; AA 255-274) and a highly conserved central part of 190 residues followed by an acidic,
glutamate-rich region. The secondary structure elements derived from the experimental structure (see Figure 4A) are shown on top of the
amino acid sequence; and the four aromatic residues (Y67, Y89, Y116, and F117) and D186 mediating the carbohydrate interaction are marked
by red crosses (Xen, Xenopus laevis 100/100; Hum, Homo sapiens 89/95; Mou, Mus musculus 86/94; Hen, Gallus gallus 84/96, Fly,
Drosophila melanogaster 41/58; Aed, Aedes aegyptii 44/62; Cae, Caenorhabditis elegans 36/58; Sch, Schistosoma japonicum 42/59; Nem,
Nematostella vectensis 51/69). The bracketed numbers represent the percentage amino acid conservation in comparison with the X. laevis
malectin protein (identities/similarities). Image published in: Schallus T et al. (2008) Copyright © 2008. Image reproduced with permission of the Publisher, American Society for Cell Biology (ASCB). This is an Open Access article. Larger Image Printer Friendly View |