1. β-Trefoil Lectins of the Family Mytilidae from a Comparative Perspective.
- Author
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Kenichi Kamata, Mayuka Ohkawa, Yuki Fujii, Yukiko Ogawa, Rajia, Sultana, Suzuna Yoshimoto, Hasan, Imtiaj, Kawsar, S. M. Abe, Ryuya Ishiwata, Shun Takakusaki, Ryuhei Hayashi, Daisuke Adachi, Takashi Hayashi, Masao Yamada, Chatterjee, Bishnu Pada, and Yasuhiro Ozeki
- Subjects
LECTINS ,MYTILIDAE ,GLYCANS - Abstract
Structural and functional differences are compared among lectins with β-trefoil folds, an essential and representative framework of proteins. The fundamental framework of this folding is the triple tandem repeat of subdomains consisting of 40 amino acids making four β-sheets to construct barrel and clover-shaped lid parts. Lectin databases UniLectin and TrefLec classified 12 categories of lectins with the β-trefoil fold in all biological domains and viruses. Each group appeared with a different proportion of distributions in each biological domain. SeviL and MytiLec represented β-trefoil lectins in the family Mytilidae. Nevertheless, each lectin had different primary structures, converging the same β-trefoil. The structural properties of MytiLec have also been shared with that of bacterial lectins. Furthermore, each mussel lectin bound to glycans of glycosphingolipid though the structures differed. Their glycan-binding properties seem to be helpful for a few applications of lectins because they recognized characteristic glycans relating to cell regulation of NK cells (GA1), auto-immune diseases (GM1b), cancers (Gb3), and regenerations (SSEA-1). [ABSTRACT FROM AUTHOR]
- Published
- 2023