Galectin-8-N-domain Recognition Mechanism for Sialylated and Sulfated Glycans*

@article{Ideo2011Galectin8NdomainRM,
  title={Galectin-8-N-domain Recognition Mechanism for Sialylated and Sulfated Glycans*},
  author={Hiroko Ideo and T. Matsuzaka and Takamasa Nonaka and Akira Seko and Katsuko Yamashita},
  journal={The Journal of Biological Chemistry},
  year={2011},
  volume={286},
  pages={11346 - 11355}
}
Galectin-8 has much higher affinity for 3′-O-sulfated or 3′-O-sialylated glycoconjugates and a Lewis X-containing glycan than for oligosaccharides terminating in Galβ1→3/4GlcNAc, and this specificity is mainly attributed to the N-terminal carbohydrate recognition domain (N-domain, CRD) (Ideo, H., Seko, A., Ishizuka, I., and Yamashita, K. (2003) Glycobiology 13, 713–723). In this study, we elucidated the crystal structures of the human galectin-8-N-domain (-8N) in the absence or presence of 4… Expand
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  • Chemistry, Medicine
  • International journal of molecular sciences
  • 2016
TLDR
Galectin-8 (Gal-8) contains two carbohydrate recognition domains (CRD) connected by a peptide linker and observation of two Gal-8 N-terminal CRD structures implies that the N-Terminal tail and the linker may influence each other’s conformation. Expand
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TLDR
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