Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 9, Issue 2, Pages 427-430Publisher
SPRINGER
DOI: 10.1007/s12104-015-9623-1
Keywords
Galectin 8; Carbohydrate recognition domain; NMR spectroscopy
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Funding
- International Human Frontier Science Program [CDA-00025/2010-C]
- National Science Council [100-2113-M-001-031-MY2, 102-2113-M-001-017-MY2]
- National Synchrotron Radiation Research Center
- Academia Sinica, Taiwan
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Galectins recognize beta-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 H-1, C-13, and N-15 chemical shift assignments of C-terminal domain of human galectin-8 (hG8C).
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