| Literature DB >> 27582340 |
Nourine A Kamili1, Connie M Arthur1, Christian Gerner-Smidt1, Eden Tafesse1, Anna Blenda1,2, Marcelo Dias-Baruffi3, Sean R Stowell1,3.
Abstract
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.Entities:
Keywords: Frontal Affinity Chromatography; Galectin; Glycan; Glycan Binding Protein; Glycoproteomics; Surface Plasmon Resonance
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Year: 2016 PMID: 27582340 PMCID: PMC5832938 DOI: 10.1002/pmic.201600116
Source DB: PubMed Journal: Proteomics ISSN: 1615-9853 Impact factor: 3.984