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All cells are coated in either glycoproteins or glycolipids, both of which help determine cell types. [7] Lectins, or proteins that bind carbohydrates, can recognize specific oligosaccharides and provide useful information for cell recognition based on oligosaccharide binding. [citation needed]
The OB-fold consists of a five-stranded β-sheet coiled to form a closed β-barrel, capped by an α-helix located at one end and a binding cleft at the other. The α-helix packs against the bottom layer of residues, roughly perpendicular to the barrel axis.
The saccharide of the glycolipid will bind to a specific complementary carbohydrate or to a lectin (carbohydrate-binding protein), of a neighboring cell. The interaction of these cell surface markers is the basis of cell recognitions, and initiates cellular responses that contribute to activities such as regulation, growth, and apoptosis. [7]
The binding of glycoproteins on the surface of parasitic cells also is believed to be a function. Several plant lectins have been found to recognize noncarbohydrate ligands that are primarily hydrophobic in nature, including adenine , auxins , cytokinin , and indole acetic acid , as well as water-soluble porphyrins .
The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...
An oligosaccharide has both a reducing and a non-reducing end. The reducing end of an oligosaccharide is the monosaccharide residue with hemiacetal functionality, thereby capable of reducing the Tollens’ reagent, while the non-reducing end is the monosaccharide residue in acetal form, thus incapable of reducing the Tollens’ reagent. [2]
In biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. [1] The binding partner of the macromolecule is often referred to as a ligand . [ 2 ]
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...