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• W2058191010 endingPage "784" @default.
• W2058191010 startingPage "773" @default.
• W2058191010 abstract "Oxidative damage to proteins leads to a variety of modifications such as racemization, carbonyl compound formation, new fluorophores, aggregation, crosslinking and insolubility, several of which are markers of pathogenesis. A particular modification that has been associated with abnormal and pathological situations is the dityrosine crosslink in proteins, thought to be responsible for the reduced solubility and elasticity of proteins, and plaque formation. Dityrosine crosslinking has been suspected to occur in the crystallins of the eye lens during cataract. We focus attention here on the generation, structure and conformational stability of such a dityrosine-linked protein of the eye lens. We find this crosslink to be readily generated photodynamically in the presence of sensitizers. Among the crystallins, crosslinking occurs most readily in the γ-crystallins under these conditions. We have isolated, purified and studied the properties of the dityrosine-linked dimer of the eye lens protein γB-crystallin. While the dityrosine crosslink does not alter the secondary structure of the protein, it changes the tertiary structure in a subtle manner. This alteration destabilizes the dimer, which denatures more readily than the parent monomer, and also makes it precipitate more readily, a point of relevance to cataractogenesis of the eye lens. Comparison of these results with those reported on other dityrosine-dimerized proteins suggests that while the conformation of these proteins might not be altered in a major manner upon dityrosine linkage, the dimer is structurally less stable and displays reduced solubility, both of which are of pathological importance." @default.
• W2058191010 created "2016-06-24" @default.
• W2058191010 creator A5016312453 @default.
• W2058191010 creator A5068824912 @default.
• W2058191010 date "1999-06-01" @default.
• W2058191010 modified "2023-09-23" @default.
• W2058191010 title "Structure and Stability of the Dityrosine-linked Dimer of γB-Crystallin" @default.
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• W2058191010 doi "https://doi.org/10.1006/exer.1999.0669" @default.
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