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- Title
β-Trefoil Lectins of the Family Mytilidae from a Comparative Perspective.
- Authors
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; Yasuhiro Ozeki
- 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).
- Subjects
LECTINS; MYTILIDAE; GLYCANS
- Publication
Trends in Carbohydrate Research, 2023, Vol 15, Issue 1, p47
- ISSN
0975-0304
- Publication type
Article