Deamidation of Human γS-Crystallin Increases Attractive Protein Interactions: Implications for Cataract
نویسندگان
چکیده
منابع مشابه
Structural analysis of the mutant protein D26G of human γS-crystallin, associated with Coppock cataract
PURPOSE To analyze the protein structural features responsible for the aggregation properties of the mutant protein D26G human γS-crystallin (HGSC) associated with congenital Coppock-type cataract. METHODS cDNAs of wild-type (WT) and D26G mutant HGSC were cloned and expressed in BL21 (DE3) pLysS cells and the proteins isolated and purified. Their secondary and tertiary structural features, ag...
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PURPOSE A recent study demonstrated the presence of protein-protein interactions among lens crystallins in a mammalian cell two-hybrid system assay and speculated about the significance of these interactions for protein solubility and lens transparency. The current study extends those findings to the following crystallin genes involved in some congenital cataracts: CRYAA (R116C), CRYAB (R120G),...
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The formation of amyloid fibrils is associated with many serious diseases as well as diverse biological functions. Despite the importance of these aggregates, predicting the aggregation propensity of a particular sequence is a major challenge. We report a joint 2D nuclear magnetic resonance (NMR) and ultraviolet (2DUV) study of fibrillization in the wild-type and two aggregation-prone mutants o...
متن کاملMultiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant
Purpose Cataract results from the formation of light-scattering precipitates due to point mutations or accumulated damage in the structural crystallins of the eye lens. Although excised cataracts are predominantly amorphous, in vitro studies show that crystallins are capable of adopting a variety of morphologies depending on the preparation method. Here we characterize thermal, pH-dependent, an...
متن کاملMechanism of cataract formation by W42R mutant human γD-crystallin
Background: The mechanism of cataract formation by the recently discovered γDcrystallin W42R mutant is unknown. Results: Structural, biochemical, and biophysical studies revealed a partially unfolded species of the W42R mutant. Conclusion: Partially unfolded species serve as nuclei for aggregation. Significance: The properties of the W42R mutant γD-crystallin provide the link to the pathogenesi...
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ژورنال
عنوان ژورنال: Biochemistry
سال: 2015
ISSN: 0006-2960,1520-4995
DOI: 10.1021/acs.biochem.5b00185