Mapping protein N-Glycosylation by COFRADIC

Abstract

The majority of proteins require co- and posttranslational modifications to become functional entities. Such modifications fulfill a plethora of tasks (e.g., modulation of enzyme activity and directing proteins to cellular compartments). One of these protein modifications that, amongst many others, plays an essential role in determining a protein&s structure and functionality is N-glycosylation, which is the enzymatic attachment of a glycan to an asparagine in the consensus motif NXS/T/C (1, 2). Next to asparagines, glycosylation can also occur on serine and threonine (O-glycosylation) (3–6) and tryptophan (C-glycosylation) (7). Protein N-glycosylation has intrinsic as well as extrinsic functions. Intrinsic functions brought about by this modification are the creation of structural modules and changes of the solubility, antigenicity and stability of the affected protein. Examples of extrinsic functions are the routing of proteins to a specific subcellular localization, and the guiding and modulation of cell adhesion and intracellular communication. [ABSTRACT FROM AUTHOR]