Structural Glycobiology Team
Team Leader
Yoshiki YAMAGUCHI (D.Pharm.)
In order to elucidate the functions of the glycans attached to proteins, it is important to analyze the glycans from the structural point of view. Our team aim to reveal the functions of glycans through the three-dimensional structures of glycoproteins and oligosaccharide-related proteins. We prepare the glycoconjugates samples with the techniques of organic synthesis and cell-engineering, and determine the three-dimensional structures using biophysical methods such as NMR or X-ray crystallography. Furthermore, we construct databases of oligosaccharide structures using bioinformatics-based approaches and decode the 'glycosignals' from the structural information. We particularly focus on disease-related glycoproteins, and develop diagnostic and therapeutic agents.
- Development of conformational analysis of glycans
- Recognition mode of glycan-binding molecules and their functions
- Construction of database on 3D structures of glycans
- December 23,2010
- 3D structure of glycoprotein-capturing lectin OS-9 elucidated
- Kanagawa, M., Satoh, T., Ikeda, A., Nakano, Y., Yagi, H., Kato, K., Kojima-Aikawa, K. and Yamaguchi, Y.:
"Crystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related beta-prism fold"
Biochem. Biophys. Res. Commun. 404, 201-205 (2011) - Satoh, T., Chen, Y., Hu, D., Hanashima, S., Yamamoto, K., and Yamaguchi, Y.:
"Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation"
Mol. Cell 40, 905-916 (2010) - Yamaguchi, Y., and Kato, K.:
"Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR Spectroscopy"
Methods in Enzymol., 478, 305-322 (2010) - Kato, K., Yamatuchi, Y., and Arata, Y.:
"Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system"
Prog. NMR Spect. 56, 346-359 (2010) - Masuda, K., Yamaguchi, Y., Takahashi, N., Jefferis R., and Kato, K;
"Mutational deglycosylation of the Fc portion of immunoglobulin G causes O-sulfation of tyrosine adjacently preceding the originally glycosylated site"
FEBS Lett. 584, 3474-3479 (2010) - Hanashima, S., Sato, K., Naito, Y., Takematsu, H., Kozutsumi, Y., Ito, Y., and Yamaguchi, Y.:
"Synthesis and binding analysis of unique AG2 pentasaccharide to human Siglec-2 using NMR techniques"
Bioorg. & Med. Chem. 18, 3720-3725 (2010) - Sato, S., Morohara. O., Fujita, D., Yamaguchi, Y., Kato, K., and Fujita, M.:
"Parallel-stacked aromatic hosts for orienting small molecules in a magnetic field: induced residual dipolar coupling by encapsulation"
J. Am. Chem. Soc., 132, 3670-3671 (2010) - Yamaguchi, Y., Hanashima, S., Yagi, H., Takahashi, Y., Sasakawa, H., Kurimoto, E., Iguchi, T., Kon, S., Ueda, T., and Kato, K.:
"NMR characterization of intramolecular interaction of osteopontin, an intrinsically disordered protein with cryptic integrin-binding motifs"
Biochem. Biophys. Res. Commun., 393, 487-491 (2010) - Yamaguchi, Y., Masuda, M., Sasakawa, H., Nonaka, T., Hanashima, S., Hisanaga, S., Kato, K., and Hasegawa, M.:
"Characterization of inhibitor-bound alpha-synuclein dimer: Role of alpha-synuclein N-terminal region in dimerization and inhibitor binding"
J. Mol. Biol., 395, 445-456 (2010) - Fujita, M., Maeda, Y., Ra, M., Yamaguchi, Y., Taguchi, R., and Kinoshita, T.:
"GPI-glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi"
Cell 139, 352-365 (2009)