The majority of protein engineers modify the structure of proteins by utilizing saturation mutagenesis, which has been systematized as the Combinatorial Active-site Saturation Test (CAST), and its expansion to Iterative Saturation Mutagenesis at locations near the binding pocket. Both of these me...
Evolutionary origins ofN-glycosylation occurring in ER have been demonstrated to be conserved among eukaryotic lineages21. We believe that diversity and novelties of PNG, and hence structures ofN-glycans of proteins in different domains of eukaryotic lives, should be reflected by gene novelties coding ...
Due to its broad spectrum of activity and its importance in the immune response IgG is one of the most studied glycoproteins –proteins that have glycans covalently attached to their polypeptide backbone. Glycans are complex oligosaccharides composed of up to 15 monosaccharide residues. Most IgG ...
Domains are functional constituents of proteins more conserved than other parts of genes in sequence, and are thus evolutionarily conserved across taxa. Genes arising by duplication-divergence is attributable enormously to domain duplication and divergence, and de novo gene births constantly give rise to...
While only about ten percent of the databank entries are defined as glycoproteins, it has been estimated recently that more than half of all proteins are g... FG Hanisch - 《Biological Chemistry》 被引量: 621发表: 2001年 O-Glycosylation of the Mucin Type : Biological Chemistry While only ...
carriers and topological similarity, i.e. the eukaryotic pathway has the same functional orientation across the membrane than several prokaryotic glycosylation pathways (Fig.1b). Despite these similarities, the homology of the proteins implicated in these pathways had never been systematically surveyed ...
Hepatitis B surface antigen (HBsAg) consists of six components of large/middle/small HBs proteins (L/M/SHBs) with non-glycosylated (ng)- or glycosylated (g)- isomers at sN146 in their shared S domain. g-SHBs plays a crucial role in hepatitis B virus (HBV) secretion. However, the host...
Variation in glycosylation among recombinant glycoproteins is not predictable and can depend on details of the biomanufacturing process as well as details of protein structure. In this study, recombinant influenza proteins were analyzed from eight strains of four different suppliers. These include five ...
These findings led to the assumption that Fc N-glycosylation influences the effector function of proteins interacting with the CH2 domain. Upon antigen binding mAbs are able to induce effector functions mediated by their Fc-part. By binding to Fc-receptors or complement proteins mAbs induce antibody...
N-GLYCOSYLATION DEFICIENCY SYNDROMES DUE TO OS ASSEMBLY DEFECTS N-glycosylation of proteins is conserved in eukaryotes. Oligosaccharide (OS)-type glycans are N-linked to proteins by the covalent amide bond between asparagine (Asn) in specific amino acid sequences (called sequons) in the nascent ...