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NMR assignments of the C-terminal domain of human galectin-8

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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 1H, 13C, and 15N chemical shift assignments of C-terminal domain of human galectin-8 (hG8C).

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Acknowledgments

The NMR spectra were obtained at the Core Facility for Protein Structural Analysis supported by National Core Facility Program for Biotechnology. STDH is a recipient of the Career Development Award (CDA-00025/2010-C) from the International Human Frontier Science Program and is supported by funding from the National Science Council (100-2113-M-001-031-MY2 and 102-2113-M-001-017-MY2), National Synchrotron Radiation Research Center and Academia Sinica, Taiwan.

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Correspondence to Shang-Te Danny Hsu.

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Liu, CH.G., Chien, CT.H., Lin, CH. et al. NMR assignments of the C-terminal domain of human galectin-8. Biomol NMR Assign 9, 427–430 (2015). https://doi.org/10.1007/s12104-015-9623-1

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  • DOI: https://doi.org/10.1007/s12104-015-9623-1

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