5XG5
Crystal structure of Mitsuba-1 with bound NAcGal
Summary for 5XG5
| Entry DOI | 10.2210/pdb5xg5/pdb |
| Descriptor | MITSUBA-1, 2-acetamido-2-deoxy-alpha-D-galactopyranose (3 entities in total) |
| Functional Keywords | protein design, lectin, de novo protein, sugar binding protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 17106.25 |
| Authors | Terada, D.,Voet, A.R.D.,Kamata, K.,Zhang, K.Y.J.,Tame, J.R.H. (deposition date: 2017-04-12, release date: 2017-07-12, Last modification date: 2024-03-27) |
| Primary citation | Terada, D.,Voet, A.R.D.,Noguchi, H.,Kamata, K.,Ohki, M.,Addy, C.,Fujii, Y.,Yamamoto, D.,Ozeki, Y.,Tame, J.R.H.,Zhang, K.Y.J. Computational design of a symmetrical beta-trefoil lectin with cancer cell binding activity. Sci Rep, 7:5943-5943, 2017 Cited by PubMed Abstract: Computational protein design has advanced very rapidly over the last decade, but there remain few examples of artificial proteins with direct medical applications. This study describes a new artificial β-trefoil lectin that recognises Burkitt's lymphoma cells, and which was designed with the intention of finding a basis for novel cancer treatments or diagnostics. The new protein, called "Mitsuba", is based on the structure of the natural shellfish lectin MytiLec-1, a member of a small lectin family that uses unique sequence motifs to bind α-D-galactose. The three subdomains of MytiLec-1 each carry one galactose binding site, and the 149-residue protein forms a tight dimer in solution. Mitsuba (meaning "three-leaf" in Japanese) was created by symmetry constraining the structure of a MytiLec-1 subunit, resulting in a 150-residue sequence that contains three identical tandem repeats. Mitsuba-1 was expressed and crystallised to confirm the X-ray structure matches the predicted model. Mitsuba-1 recognises cancer cells that express globotriose (Galα(1,4)Galβ(1,4)Glc) on the surface, but the cytotoxicity is abolished. PubMed: 28724971DOI: 10.1038/s41598-017-06332-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
Download full validation report
