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Budowa i synteza glikopeptydów

Warianty tytułu
EN
Structure and synthesis glycopeptides
Języki publikacji
PL
Abstrakty
EN
During the past decades it has been recognized that most of the natural proteins of mammals carry covalently linked saccharide side chains. The carbohydrate portions of the glycoproteins as well as those of glycolipids obviously play key roles in biological recognition processes. A glycoprotein is a compound containing carbohydrate (or glycan) covalently linked to protein. The carbohydrate may be in a form of monosaccharide, disaccharide(s), oligosaccharide(s), polysaccharide(s), or their derivatives (e.g. sulfo- or phos-pho-substituted). One, a few, or many carbohydrate units may be present. There are two most common types of glycoproteins: O- and N-glycoproteins. In eukaryotes, the most prevalent type of O-linked glycosylation is the mucin-type glycosylation, where N-acetyl-D-galactosamine (GalNAc) is linked in an ?-anomeric configuration to the ?-hydroxyl group of either a serine or a threonine residue of the polypeptide. Other types of O-linked glycosylation include glycosaminoglycans, such as heparin and chondrotin sulfate, which are attached to the polypeptide chain through ?-linked xylose residues. An older and more prevalent type of glycosylation, N-linked glycosylation, is found in a wide range of organisms ranging from Archae to mammals and other eukaryotes. N-Glycosylation is a modification performed cotranslationally (during the translation of mRNA to protein) and is available to any secreted or membrane-bound protein containing the triplet amino acid sequence AsnXxxSer/Thr (where Xxx is any amino acid except Pro). An oligosaccharide is transferred to the amide side chain of Asn from a dolichol phosphate glycosyl donor, by the action of mem-brane-bound oligosaccharyl transferase in the endoplasmic reticulum (ER). The fully translated glycoprotein is then subject to glycan trimming and processing which is further elaborated in the ER and Golgi apparatus.
Rocznik
Strony
79--98
Opis fizyczny
bibliogr. 24 poz., tab., wykr.
Twórcy
autor
autor
autor
Bibliografia
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bwmeta1.element.baztech-article-BUS5-0002-0014