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The Structure and Stability of the Disulfide-Linked ?S-Crystallin Dimer Provide Insight into Oxidation Products Associated with Lens Cataract Formation

Thorn, David; Grosas, Aidan; Mabbitt, Peter; Ray, Nicholas; Jackson, Colin; Carver, John

Description

The reducing environment in the eye lens diminishes with age, leading to significant oxidative stress. Oxidation of lens crystallin proteins is the major contributor to their destabilization and deleterious aggregation that scatters visible light, obscures vision, and ultimately leads to cataract. However, the molecular basis for oxidation-induced aggregation is unknown. Using X-ray crystallography and small-angle X-ray scattering, we describe the structure of a disulfide-linked dimer of human...[Show more]

CollectionsANU Research Publications
Date published: 2019
Type: Journal article
URI: http://hdl.handle.net/1885/202479
Source: Journal of Molecular Biology
DOI: 10.1016/j.jmb.2018.12.005

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