4WVV

Chicken Galectin-8 N-terminal domain complexed with lactose

Summary for 4WVV

• Entry DOI: 10.2210/pdb4wvv/pdb
• Related PRD ID: PRD_900008
• Descriptor: Galectin, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: lectin, carbohydrate recognition domain, sugar binding protein
• Biological source: Gallus gallus (Chicken)
• Total number of polymer chains: 1
• Total formula weight: 16980.68

Authors

Ruiz, F.M.,Romero, A. (deposition date: 2014-11-07, release date: 2015-09-23, Last modification date: 2024-01-10)

Primary citation

Ruiz, F.M.,Gilles, U.,Lindner, I.,Andre, S.,Romero, A.,Reusch, D.,Gabius, H.J.
Combining Crystallography and Hydrogen-Deuterium Exchange to Study Galectin-Ligand Complexes.
Chemistry, 21:13558-13568, 2015

PubMed Abstract: 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.

PubMed: 26270612
DOI: 10.1002/chem.201501961

Experimental method

X-RAY DIFFRACTION (1.205 Å)