Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage.

ABSTRACT: Divalent metal cations can play a role in protein aggregation diseases, including cataract. Here we compare the aggregation of human γS-crystallin, a key structural protein of the eye lens, via mutagenesis, ultraviolet light damage, and the addition of metal ions. All three aggregation pathways result in globular, amorphous-looking structures that do not elongate into fibers. We also investigate the molecular mechanism underlying copper(II)-induced aggregation. This work was motivated by the observation that zinc(II)-induced aggregation of γS-crystallin is driven by intermolecular bridging of solvent-accessible cysteine residues, while in contrast, copper(II)-induced aggregation of this protein is exacerbated by the removal of solvent-accessible cysteines via mutation. Here we find that co

SUBMITTER: Roskamp KW 

PROVIDER: S-EPMC7732359 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature