Abstract
Two galectins isolated from the skin mucus of conger eel (Conger myriaster), named congerins I and II, are dimers composed of two identical subunits of 136 and 135 amino acid residues, respectively. They belong to the proto-type galectins and showed 48% sequence identity and different thermal stabilities and different sugar binding. The molecular evolutionary analyses and X-ray crystallography analyses of congerins I and II reveal that they have evolved in an accelerating and adaptive manner to the emergence of a new structure including domain-swapping manner and a unique new ligand-binding site. In this review, we summarize and discuss the structure-properties/function relationships and the molecular evolution of fish galectins.
Original language | English |
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Pages (from-to) | 177-187 |
Number of pages | 11 |
Journal | Trends in Glycoscience and Glycotechnology |
Volume | 14 |
Issue number | 77 |
DOIs | |
Publication status | Published - 2002 May |
Keywords
- Adaptive evolution
- Conger eel
- Domain swapping
- Galectin
- X-ray crystallography
ASJC Scopus subject areas
- Biochemistry
- Organic Chemistry