Alternative glycosylation modulates function of IgG and other proteins — Implications on evolution and disease

• Published in: Biochimica et biophysica acta Vol. 1820; no. 9; pp. 1318 - 1326
• Main Authors: Gornik, Olga, Pavić, Tamara, Lauc, Gordan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2012
• Subjects: Animals; biochemical pathways; Biological Evolution; Biosynthetic Pathways - physiology; Disease; Disease - etiology; DNA; enzymes; Evolution; genes; Glycan; Glycome; Glycoprotein; Glycoproteins - chemistry; Glycoproteins - metabolism; Glycoproteins - physiology; Glycosylation; Humans; immunoglobulin G; Immunoglobulin G - chemistry; Immunoglobulin G - metabolism; Immunoglobulin G - physiology; Models, Biological; mutation; polysaccharides; Polysaccharides - metabolism; Protein glycosylation; protein structure; Structure-Activity Relationship; Evolution; Protein glycosylation; Disease; Glycome; Glycan; Glycoprotein

Nearly all membrane and secreted proteins, as well as numerous intracellular proteins are glycosylated. However, contrary to proteins which are defined by their individual genetic templates, glycans are encoded in a complex dynamic network of hundreds of genes which participate in the complex biosyn...