| Literature DB >> 26126590 |
Chun-Hao Gerard Liu1,2,3, Chih-Ta Henry Chien1,4, Chun-Hung Lin1,4,5, Shang-Te Danny Hsu6,7.
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).Entities:
Keywords: Carbohydrate recognition domain; Galectin 8; NMR spectroscopy
Mesh:
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Year: 2015 PMID: 26126590 DOI: 10.1007/s12104-015-9623-1
Source DB: PubMed Journal: Biomol NMR Assign ISSN: 1874-270X Impact factor: 0.746