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TitleThe Structure and Stability of the Disulfide-Linked γS-Crystallin Dimer Provide Insight into Oxidation Products Associated with Lens Cataract Formation.
Journal, issue, pagesJ Mol Biol, Vol. 431, Issue 3, Page 483-497, Year 2019
Publish dateFeb 1, 2019
AuthorsDavid C Thorn / Aidan B Grosas / Peter D Mabbitt / Nicholas J Ray / Colin J Jackson / John A Carver /
PubMed AbstractThe 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 ...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 γS-crystallin that was obtained via oxidation of C24. The γS-crystallin dimer is stable at glutathione concentrations comparable to those in aged and cataractous lenses. Moreover, dimerization of γS-crystallin significantly increases the protein's propensity to form large insoluble aggregates owing to non-cooperative domain unfolding, as is observed in crystallin variants associated with early-onset cataract. These findings provide insight into how oxidative modification of crystallins contributes to cataract and imply that early-onset and age-related forms of the disease share comparable development pathways.
External linksJ Mol Biol / PubMed:30552875
MethodsSAS (X-ray in house) / X-ray diffraction
Resolution2.1 Å
Structure data

SASDE27:
Gamma-crystallin S monomer (Gamma-crystallin S)
Method: SAXS/SANS

SASDEZ6:
Gamma-crystallin S disulfide-linked dimer (Gamma-crystallin S)
Method: SAXS/SANS

PDB-6fd8:
Gamma-s crystallin dimer
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / Crystallin / eye lens / vision / cataract.

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