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Key regulators of galectin–glycan interactions
Author(s) -
Kamili Nourine A.,
Arthur Connie M.,
GernerSmidt Christian,
Tafesse Eden,
Blenda Anna,
DiasBaruffi Marcelo,
Stowell Sean R.
Publication year - 2016
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201600116
Subject(s) - galectin , glycan , glycosylation , computational biology , microbiology and biotechnology , biology , receptor , chemistry , biochemistry , glycoprotein
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.