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NMR assignments of the C-terminal domain of human galectin-8 |
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| Authors: | Chun-Hao?Gerard?Liu,Chih-Ta?Henry?Chien,Chun-Hung?Lin,Shang-Te?Danny?Hsu author-information" > author-information__contact u-icon-before" > mailto:sthsu@gate.sinica.edu.tw" title=" sthsu@gate.sinica.edu.tw" itemprop=" email" data-track=" click" data-track-action=" Email author" data-track-label=" " >Email author |
| Affiliation: | 1.Institute of Biological Chemistry,Academia Sinica,Taipei,Taiwan;2.Institue of Bioinformatics and Structural Biology,National Tsin Hua University,Hsinchu,Taiwan;3.Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program,Academia Sinica,Nankang, Taipei,Taiwan;4.Department of Chemistry,National Taiwan University,Taipei,Taiwan;5.Institute of Biochemical Science,National Taiwan University,Taipei,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 1H, 13C, and 15N chemical shift assignments of C-terminal domain of human galectin-8 (hG8C). |
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