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Conformational change of a unique sequence in a fungal galectin from Agrocybe cylindracea controls glycan ligand‐binding specificity
Author(s) -
Kuwabara Naoyuki,
Hu Dan,
Tateno Hiroaki,
Makyio Hisayoshi,
Hirabayashi Jun,
Kato Ryuichi
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.08.046
Subject(s) - glycan , galectin , mutant , biochemistry , conformational change , sequence (biology) , binding site , galactose , galectin 3 , biology , galectin 1 , plasma protein binding , binding affinities , chemistry , computational biology , stereochemistry , microbiology and biotechnology , receptor , gene , glycoprotein , immunology
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.