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For instance, some proteins do not fold correctly unless they are glycosylated. [2] In other cases, proteins are not stable unless they contain oligosaccharides linked at the amide nitrogen of certain asparagine residues. The influence of glycosylation on the folding and stability of glycoprotein is twofold. Firstly, the highly soluble glycans ...
Hinge regions of immunoglobulins contain highly O-glycosylated regions between individual domains to maintain their structure, allow interactions with foreign antigens and protect the region from proteolytic cleavage. [1] [8] Alzheimer's may be affected by O-glycosylation. Tau, the protein that accumulates to cause neurodegeneration in ...
Domain I (residues 1–27 and 383–414) forms a three-stranded anti-parallel β-sheet. This domain contains two disulfide bridges that are necessary for correct folding, as well as a glycosylated residue (Asn19) that is required for catalytic activity in vivo.
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 ...
The resulting GPI-anchored proteins play key roles in a wide variety of biological processes. [1] GPI is composed of a phosphatidylinositol group linked through a carbohydrate -containing linker ( glucosamine and mannose glycosidically bound to the inositol residue) and via an ethanolamine phosphate (EtNP) bridge to the C-terminal amino acid of ...
CD68 (also called gp110 or macrosialin) [5] is a heavily glycosylated integral membrane protein whose structure consists of a mucin-like domain followed by a proline-rich hinge; a single LAMP-like domain; a transmembrane region and a short cytoplasmic tail. CD molecules are leucocyte antigens on cell surfaces.
Proteoglycans are proteins [1] that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein " with one or more covalently attached glycosaminoglycan (GAG) chain(s). [ 2 ] The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate ...
The KR (keto-reductase) domain reduces the β-keto group to a β-hydroxy group, the DH (dehydratase) domain splits off H 2 O, resulting in the α-β-unsaturated alkene, and the ER (enoyl-reductase) domain reduces the α-β-double-bond to a single-bond. These modification domains actually affect the previous addition to the chain (i.e. the group ...