期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 48, 期 3, 页码 1255-1268出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST20200311
关键词
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资金
- Agencia Nacional de Promocion Cientifica y Tecnologica [PICT-2007-1631, PICT-2012-0071, PICT-2015-0564]
- Fundacion Sales
- Fundacion Rene Baron
- Fundacion Bunge Born
Galectin-8 (Gal-8) is a tandem-repeat type galectin with affinity for beta-galactosides, bearing two carbohydrate recognition domains (CRD) connected by a linker peptide. The N- and C-terminal domains (Gal-8N and Gal-8C) share 35% homology, and their glycan ligand specificity is notably dissimilar: while Gal-8N shows strong affinity for alpha(2-3)-sialylated oligosaccharides, Gal-8C has higher affinity for non-sialylated oligosaccharides, including poly-N-acetyllactosamine and/or A and B blood group structures. Particularly relevant for understanding the biological role of this lectin, full-length Gal-8 can bind cell surface glycoconjugates with broader affinity than the isolated Gal-8N and Gal-8C domains, a trait also described for other tandem-repeat galectins. Herein, we aim to discuss the potential use of separate CRDs in modelling tandem-repeat galectin-8 and its biological functions. For this purpose, we will cover several aspects of the structure-function relationship of this protein including crystallographic structures, glycan specificity, cell function and biological roles, with the ultimate goal of understanding the potential role of each CRD in predicting full-length Gal-8 involvement in relevant biological processes.
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