期刊
PROTEOMICS
卷 16, 期 24, 页码 3111-3125出版社
WILEY
DOI: 10.1002/pmic.201600116
关键词
Frontal Affinity Chromatography; Galectin; Glycan; Glycan Binding Protein; Glycoproteomics; Surface Plasmon Resonance
资金
- NIGMS NIH HHS [T32 GM008169] Funding Source: Medline
- NIH HHS [DP5 OD019892] Funding Source: Medline
Protein-ligand interactions serve as fundamental regulators of numerous biological processes. Among protein-ligand pairs, glycan binding proteins (GBPs) and the glycans they recognize represent unique and highly complex interactions implicated in a broad range of regulatory activities. With few exceptions, cell surface receptors and secreted proteins are heavily glycosylated. As these glycans often represent highly regulatable post-translational modifications, alterations in glycosylation can fundamentally impact GBP recognition. Among GBPs, galectins in particular appear to engage a diverse set of glycan determinants to impact a broad range of biological processes. In this review, we will explore factors that impact galectin activity, including the effect of glycan modification on galectin-glycan interactions.
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