6LF2

SeviL bound to asialo-GM1 saccharide

6LF2 の概要

• エントリーDOI: 10.2210/pdb6lf2/pdb
• 分子名称: SeviL, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: trefoil, anti-cancer, apoptosis, mussel, sugar binding protein
• 由来する生物種: Septifer virgatus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32109.49

構造登録者

Kamata, K.,Ozeki, Y.,Park, S.-Y.,Tame, J.R.H. (登録日: 2019-11-28, 公開日: 2020-12-02, 最終更新日: 2023-11-22)

主引用文献

Kamata, K.,Mizutani, K.,Takahashi, K.,Marchetti, R.,Silipo, A.,Addy, C.,Park, S.Y.,Fujii, Y.,Fujita, H.,Konuma, T.,Ikegami, T.,Ozeki, Y.,Tame, J.R.H.
The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata.
Sci Rep, 10:22102-22102, 2020

PubMed Abstract: SeviL is a recently isolated lectin found to bind to the linear saccharides of the ganglioside GM1b (Neu5Ac[Formula: see text](2-3)Gal[Formula: see text](1-3)GalNAc[Formula: see text](1-4)Gal[Formula: see text](1-4)Glc) and its precursor, asialo-GM1 (Gal[Formula: see text](1-3)GalNAc[Formula: see text](1-4)Gal[Formula: see text](1-4)Glc). The crystal structures of recombinant SeviL have been determined in the presence and absence of ligand. The protein belongs to the [Formula: see text]-trefoil family, but shows only weak sequence similarity to known structures. SeviL forms a dimer in solution, with one binding site per subunit, close to the subunit interface. Molecular details of glycan recognition by SeviL in solution were analysed by ligand- and protein-based NMR techniques as well as ligand binding assays. SeviL shows no interaction with GM1 due to steric hindrance with the sialic acid branch that is absent from GM1b. This unusual specificity makes SeviL of great interest for the detection and control of certain cancer cells, and cells of the immune system, that display asialo-GM1.

PubMed: 33328520
DOI: 10.1038/s41598-020-78926-7

実験手法

X-RAY DIFFRACTION (1.6 Å)