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At physiological pH, CRYGD forms aggregates that look amorphous and disordered by electron microscopy. Surprisingly, solid-state NMR reveals that these amorphous deposits have a high degree of structural homogeneity at the atomic level and that the aggregated protein retains a native-like conformation, with no evidence for large-scale misfolding.
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A molecular dynamics approach to explore the structural characterization of cataract causing mutation R58H on human gammaD crystallin.
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This research compared the effects of various glycation modifiers on Hgammad-crystallin aggregation, by treating samples of Hgammad-crystallin with ribose, galactose, or methylglyoxal using several biophysical techniques
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Study reports the identification of Cys111 as the major residue responsible for disulfide formation in protein dimers as well as for Cu2+-induced aggregation of human gammaD-crystallin.
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Using the P23T mutant of gammaD-crystallin, a protein associated with congenital cataract, we have demonstrated that the equilibrium solubility boundary and solution behavior measured using phase diagrams of purified protein solutions is consistent with the assembly of the protein expressed in cell-free expression medium in artificial cells (without fluorescent labelling) and condensates formed in mammalian cells.
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we identified two heterozygous rare variants in genes that are involved in early cataract development; the novel c.809C>A; p.(Ser270Tyr) in MAF and the c.168C>G; p.(Tyr56 *) variant in CRYGD, previously reported as pathogenic
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Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.
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the mechanism of aggregation of two gammaD-crystallin mutants, W42R and W42Q: the former a congenital cataract mutation
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Mutational analysis of CRYGD identified a recurrent (p.P24T) mutation in two unrelated families with congenital coralliform cataracts and three novel (p.Q101X, p.E104fsX4 and p.E135X) mutations in three families with congenital nuclear cataracts.
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The nonsense mutation c.471G>A of the CRYGD gene probably underlies the congenital cataract in the pedigree
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Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human gammaD-Crystallin Protein.
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We have identified a novel mutation, c.451_452insGACT, in CRYGD, which is associated with nuclear cataract. This is the first insertion mutation of CRYGD found to cause autosomal dominant congenital cataract.
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We have used trio-based exome sequencing to uncover a recurrent missense mutation in CRYGD and two novel missense mutations in GJA8 associated with autosomal dominant cataract in three nuclear families.
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Created are three double mutants of human gamma D-crystallin for which the phase diagrams for singly mutated proteins can be used to predict the behavior of the double mutants.
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oxidation-mimicking W42Q mutant of gammad-crystallin formed non-native polymers starting from a native-like state under physiological conditions
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Shared epitopes and smoking were associated with the production of anti-CCP antibodies and rheumatoid factors of IgM and IgA isotypes, which again were associated with erosive disease at presentation only in smokers.
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The presence of anti-CCP antibodies was a reliable serologic marker in rheumatoid arthritis diagnosis and was associated with cigarette smoking.
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These results indicated that the single lysine residue at the second position (K2) is acetylated at an early age and that the amount of K2-acetylated gamma D-crystallin increased with age.
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Results show that thermal denaturation of gammaD-crystallin results in sheet-like aggregates that contain cross-linked oligomers of the protein.
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This study identified a novel congenital nuclear and posterior polar cataract phenotype caused by the recurrent mutation p. R140X in CRYGD.
