Elderberry bark lectins evolved to recognize Neu5Ac alpha2,6Gal/GalNAc sequence from a Gal/GalNAc binding lectin through the substitution of amino-acid residues critical for the binding to sialic acid.

@article{Kaku2007ElderberryBL,
  title={Elderberry bark lectins evolved to recognize Neu5Ac alpha2,6Gal/GalNAc sequence from a Gal/GalNAc binding lectin through the substitution of amino-acid residues critical for the binding to sialic acid.},
  author={H. Kaku and Hiroki Kaneko and Naoto Minamihara and K. Iwata and E. Jordan and M. Rojo and Naoko Minami-Ishii and E. Minami and S. Hisajima and N. Shibuya},
  journal={Journal of biochemistry},
  year={2007},
  volume={142 3},
  pages={
          393-401
        }
}
Bark lectins from the elderberry plants belonging to the genus Sambucus specifically bind to Neu5Acalpha2,6Gal/GalNAc sequence and have long been used for the analysis of sialoglycoconjugates that play important roles in many biological phenomena. However, molecular basis of such a unique carbohydrate binding specificity has not been understood. To answer these questions, we tried to identify the amino-acid residues in the Japanese elderberry bark lectin, Sambucus sieboldiana agglutinin that… Expand
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