4wvw

Chicken Galectin-8 N-terminal domain complexed with 3'-sialyl-lactose

spinqualitylabelsall models 4wvw, resolution 1.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wvw is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.47Å Ligands: GAL, GLC, PEG, PRD_900025, SIA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1W2P6_CHICK Publication Abstract from PubMed 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 alpha-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. Combining Crystallography and Hydrogen-Deuterium Exchange to Study Galectin-Ligand Complexes.,Ruiz FM, Gilles U, Lindner I, Andre S, Romero A, Reusch D, Gabius HJ Chemistry. 2015 Sep 21;21(39):13558-68. doi: 10.1002/chem.201501961. Epub 2015, Aug 13. PMID:26270612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galectin 3D structures

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