N-Glycosylation as a Modulator of Protein Conformation and Assembly in Disease.

ABSTRACT: Glycosylation, a prevalent post-translational modification, plays a pivotal role in regulating intricate cellular processes by covalently attaching glycans to macromolecules. Dysregulated glycosylation is linked to a spectrum of diseases, encompassing cancer, neurodegenerative disorders, congenital disorders, infections, and inflammation. This review delves into the intricate interplay between glycosylation and protein conformation, with a specific focus on the profound impact of N-glycans on the selection of distinct protein conformations characterized by distinct interactomes-namely, protein assemblies-under normal and pathological conditions across various diseases. We begin by examining the spike protein of the SARS virus, illustrating how N-glycans regulate the infectivity of pathogen

SUBMITTER: Pasala C 

PROVIDER: S-EPMC10968129 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature