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Combining Crystallography and Hydrogen–Deuterium Exchange to Study Galectin–Ligand Complexes
Author(s) -
Ruiz Federico M.,
Gilles Ulrich,
Lindner Ingo,
André Sabine,
Romero Antonio,
Reusch Dietmar,
Gabius HansJoachim
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201501961
Subject(s) - galectin , chemistry , glycan , ligand (biochemistry) , galectin 3 , hydrogen–deuterium exchange , cell adhesion , glycoprotein , biochemistry , hydrogen , cell , receptor , biology , organic chemistry , immunology
The physiological significance arising from translating information stored in glycans into cellular effects explains the interest in structurally defining lectin–carbohydrate recognition. The relatively small set of adhesion/growth‐regulatory galectins in chicken makes this system attractive to study the origins of specificity and divergence. Cell binding by using glycosylation mutants reveals binding of the N‐terminal domain of chicken galectin‐8 (CG‐8N) to α‐2,3‐sialylated and galactose‐terminated glycan chains. Cocrystals with lactose and its 3′‐sialylated derivative disclose Arg58 as a key contact for the carboxylic acid and differences in loop lengths to the three homodimeric chicken galectins. Monitoring hydrogen–deuterium exchange by mass spectrometry revealed an effective reduction of deuteration after ligand binding within the contact area. In addition, evidence for changes in solvent accessibility of amide protons beyond this site was obtained. Their detection, which highlights the sensor capacity of this technique, encourages systematic studies on galectins and beyond.