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Updated: Jun 20, 2026
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Crystallization and preliminary structural studies of champedak galactose-binding lectin
Mads Gabrielsen1, Alan Riboldi-Tunnicliffe, Puteri Shafinaz Abdul-Rahman
1Division of Molecular and Cellular Biology, Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow, Scotland. m.gabrielsen@bio.gla.ac.uk
Abstract:
Galactose-binding lectin from champedak (Artocarpus integer) consists of two chains: alpha and beta (133 and 21 amino acids, respectively). It has been shown to recognize and bind to carbohydrates involved in IgA and C1 inhibitor molecules. The protein was purified and crystallized at 293 K. Crystals were observed in two space groups, P2(1) and P2(1)2(1)2, and diffracted to 1.65 and 2.6 A, respectively.
