Allosteric regulation of the carbohydrate-binding ability of a novel conger eel galectin by D-mannoside.

ABSTRACT: Conger eel has two galectins, termed congerins I and II (Con I and II), that function in mucus as biodefense molecules. Con I and II have acquired a novel protein fold via domain swapping and a new ligand-binding site by accelerated evolution, which enables recognition of some marine bacteria. In this study, we identified a new congerin isotype, congerin P (Con-P), from the peritoneal cells of conger eel. Although Con-P displayed obvious homology with galectins, we observed substitution of 7 out of 8 amino acid residues in the carbohydrate recognition domain that are conserved in all other known galectins. To understand the structure-function relationships of this unique galectin, recombinant Con-P was successfully expressed in Escherichia coli by using a Con II-tagged fusion protein syste

SUBMITTER: Watanabe M 

PROVIDER: S-EPMC3438938 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature