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3VV1

Crystal Structure of Caenorhabditis elegans galectin LEC-6

3VV1 の概要
エントリーDOI10.2210/pdb3vv1/pdb
分子名称Protein LEC-6, beta-D-galactopyranose-(1-4)-alpha-L-fucopyranose, MAGNESIUM ION, ... (4 entities in total)
機能のキーワードgalectin, galactose-1, 4-fucose binding, sugar binding protein
由来する生物種Caenorhabditis elegans (nematode)
タンパク質・核酸の鎖数2
化学式量合計35700.09
構造登録者
Makyio, H.,Takeuchi, T.,Tamura, M.,Nishiyama, K.,Takahashi, H.,Natsugari, H.,Arata, Y.,Kasai, K.,Yamada, Y.,Wakatsuki, S.,Kato, R. (登録日: 2012-07-10, 公開日: 2013-05-22, 最終更新日: 2024-03-20)
主引用文献Makyio, H.,Takeuchi, T.,Tamura, M.,Nishiyama, K.,Takahashi, H.,Natsugari, H.,Arata, Y.,Kasai, K.,Yamada, Y.,Wakatsuki, S.,Kato, R.
Structural basis of preferential binding of fucose-containing saccharide by the Caenorhabditis elegans galectin LEC-6
Glycobiology, 23:797-805, 2013
Cited by
PubMed 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.
PubMed: 23481096
DOI: 10.1093/glycob/cwt017
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 3vv1
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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