3WMV
The structure of an anti-cancer lectin mytilec with ligand from the mussel Mytilus galloprovincialis
Summary for 3WMV
| Entry DOI | 10.2210/pdb3wmv/pdb |
| Related | 3WMU |
| Descriptor | Lectin, 2-acetamido-2-deoxy-alpha-D-galactopyranose (3 entities in total) |
| Functional Keywords | sugar binding protein, lectin, carbohydrate |
| Biological source | Mytilus galloprovincialis (Mediterranean mussel) |
| Total number of polymer chains | 2 |
| Total formula weight | 35718.48 |
| Authors | Terada, D.,Kawai, F.,Noguchi, H.,Unzai, S.,Park, S.-Y.,Ozeki, Y.,Tame, J.R.H. (deposition date: 2013-11-27, release date: 2014-12-03, Last modification date: 2024-03-20) |
| Primary citation | Terada, D.,Kawai, F.,Noguchi, H.,Unzai, S.,Hasan, I.,Fujii, Y.,Park, S.-Y.,Ozeki, Y.,Tame, J.R.H. Crystal structure of MytiLec, a galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types Sci Rep, 6:28344-28344, 2016 Cited by PubMed Abstract: MytiLec is a lectin, isolated from bivalves, with cytotoxic activity against cancer cell lines that express globotriaosyl ceramide, Galα(1,4)Galβ(1,4)Glcα1-Cer, on the cell surface. Functional analysis shows that the protein binds to the disaccharide melibiose, Galα(1,6)Glc, and the trisaccharide globotriose, Galα(1,4)Galβ(1,4)Glc. Recombinant MytiLec expressed in bacteria showed the same haemagglutinating and cytotoxic activity against Burkitt's lymphoma (Raji) cells as the native form. The crystal structure has been determined to atomic resolution, in the presence and absence of ligands, showing the protein to be a member of the β-trefoil family, but with a mode of ligand binding unique to a small group of related trefoil lectins. Each of the three pseudo-equivalent binding sites within the monomer shows ligand binding, and the protein forms a tight dimer in solution. An engineered monomer mutant lost all cytotoxic activity against Raji cells, but retained some haemagglutination activity, showing that the quaternary structure of the protein is important for its cellular effects. PubMed: 27321048DOI: 10.1038/srep28344 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.05 Å) |
Structure validation
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