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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
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Galectin-3 interactions with glycosphingolipids.

Patrick M Collins1, Khuchtumur Bum-Erdene1, Xing Yu1

  • 1Institute for Glycomics, Griffith University Gold Coast Campus, Queensland 4222, Australia.

Journal of Molecular Biology
|December 12, 2013
PubMed
Summary
This summary is machine-generated.

This study reveals the atomic details of galectin-3 binding to key glycosphingolipids, showing distinct interactions with gangliosides versus lacto/neolacto-series. These findings are crucial for understanding galectin-3

Keywords:
X-ray structurescarbohydrate recognitiongalectingangliosideglycosphingolipid

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Area of Science:

  • Structural Biology
  • Glycobiology
  • Molecular Interactions

Background:

  • Galectins, particularly galectin-3, play significant roles in various pathological conditions, including cancer and inflammation.
  • Mammalian cells express lacto-, neolacto-, and ganglio-series glycosphingolipids, which serve as endogenous receptors for galectins.
  • Key structural components of these glycosphingolipids include lacto-N-tetraose (LNT) and lacto-N-neotetraose (LNnT).

Purpose of the Study:

  • To elucidate the atomic-level interactions between human galectin-3 and core glycosphingolipid structures.
  • To investigate the binding modes of galectin-3 with LNT, LNnT, and a ganglioside (α-GM3).
  • To understand how galectin-3's ligand affinity is influenced by its wild type and K176L mutant forms.

Main Methods:

  • X-ray crystallography was employed to determine the structures of human galectin-3 (wild type and K176L mutant) in complex with LNT, LNnT, and α-GM3.
  • Analysis of the bound ligand orientations and interactions within the carbohydrate recognition domain of galectin-3.
  • Comparison of binding modes across different glycosphingolipid series.

Main Results:

  • Galectin-3 exhibits distinct binding modes for gangliosides compared to lacto/neolacto-glycosphingolipids.
  • Recognition of the core β-galactoside region is challenged in gangliosides when embedded in larger glycans.
  • Different orientations of terminal galactose in galectin-3-bound LNT and LNnT impact interactions with higher-order glycosphingolipids and poly-N-acetyllactosamine structures.

Conclusions:

  • These structures provide the first atomic insights into galectin-3's interactions with core mammalian glycosphingolipid structures.
  • Understanding these interactions is vital for comprehending galectin-3's role in diseases where it engages with these receptors.
  • The findings offer a basis for exploring galectin-3 as a therapeutic target in cancer and other pathologies.