Conformational change of a unique sequence in a fungal galectin from Agrocybe cylindracea controls glycan ligand-binding specificity

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Abstract

A fungal galectin from Agrocybe cylindracea (ACG) exhibits broad binding specificity for β-galactose-containing glycans. We determined the crystal structures of wild-type ACG and the N46A mutant, with and without glycan ligands. From these structures and a saccharide-binding analysis of the N46A mutant, we revealed that a conformational change of a unique insertion sequence containing Asn46 provides two binding modes for ACG, and thereby confers broad binding specificity. We propose that the unique sequence provides these two distinct glycan-binding modes by an induced-fit mechanism. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Kuwabara, N., Hu, D., Tateno, H., Makyio, H., Hirabayashi, J., & Kato, R. (2013). Conformational change of a unique sequence in a fungal galectin from Agrocybe cylindracea controls glycan ligand-binding specificity. FEBS Letters, 587(22), 3620–3625. https://doi.org/10.1016/j.febslet.2013.08.046

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