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Updated: Aug 1, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
NMR assignments of the C-terminal domain of human galectin-8
Chun-Hao Gerard Liu1,2,3, Chih-Ta Henry Chien1,4, Chun-Hung Lin1,4,5
1Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan.
Abstract:
Galectins recognize β-galectosides to promote a variety of cellular functions. Despite their sequence variations, all galectins share the same carbohydrate recognition domains (CRD) and their modes of ligand recognition at a structural level are essentially identical. Human galectin 8 plays an important role in numerous cancer and immune responses. It consists of two CRDs that are connected via a flexible linker. The substrate affinities and specificities of the N- and C-terminal domains are quite different. In order to investigate the structural basis of their substrate specificities, we complete the NMR (1)H, (13)C, and (15)N chemical shift assignments of C-terminal domain of human galectin-8 (hG8C).
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