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- Title
Structural basis of preferential binding of fucose-containing saccharide by the Caenorhabditis elegans galectin LEC-6.
- Authors
Makyio, Hisayoshi; Takeuchi, Tomoharu; Tamura, Mayumi; Nishiyama, Kazusa; Takahashi, Hideyo; Natsugari, Hideaki; Arata, Yoichiro; Kasai, Ken-ichi; Yamada, Yusuke; Wakatsuki, Soichi; Kato, Ryuichi
- Abstract
Galectins are a group of lectins that can bind carbohydrate chains containing β-galactoside units. LEC-6, a member of galectins of Caenorhabditis elegans, binds fucose-containing saccharides. We solved the crystal structure of LEC-6 in complex with galactose-β1,4-fucose (Galβ1-4Fuc) at 1.5 Å resolution. The overall structure of the protein and the identities of the amino-acid residues binding to the disaccharide are similar to those of other galectins. However, further structural analysis and multiple sequence alignment between LEC-6 and other galectins indicate that a glutamic acid residue (Glu67) is important for the preferential binding between LEC-6 and the fucose moiety of the Galβ1-4Fuc unit. Frontal affinity chromatography analysis indicated that the affinities of E67D and E67A mutants for Galβ1-4Fuc are lower than that of wild-type LEC-6. Furthermore, the affinities of Glu67 mutants for an endogenous oligosaccharide, which contains a Galβ1-4Fuc unit, are drastically reduced relative to that of the wild-type protein. We conclude that the Glu67 in the oligosaccharide-binding site assists the recognition of the fucose moiety by LEC-6.
- Subjects
FUCOSE; SACCHARIDES; CAENORHABDITIS elegans; GALECTINS; LECTINS; CARBOHYDRATES; CRYSTAL structure; OLIGOSACCHARIDE structure
- Publication
Glycobiology, 2013, Vol 23, Issue 7, p797
- ISSN
0959-6658
- Publication type
Article
- DOI
10.1093/glycob/cwt017