ArticleStructure (London, England : 1993)2013
Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Human Crystallin Variation and Cataract.Investigative ophthalmology & visual science · 2026Review
- Mimicking oxidative damage in γS-crystallin with site-specific incorporation of 5-hydroxytryptophan.Biophysical reports · 2026Article
- Investigation of the Effect of C-Terminal Adjacent Phenylalanine Residues on Asparagine Deamidation by Quantum Chemical Calculations.International journal of molecular sciences · 2025Article
- Mini-αA-crystallin protects a client lens protein from catastrophic aggregation due to heat stress.Protein science : a publication of the Protein Society · 2025Article
- Characterization of the Interaction of Human γS Crystallin with Metal Ions and Its Effect on Protein Aggregation.Biomolecules · 2024Article
- In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate.International journal of molecular sciences · 2024Review
- Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract.International journal of molecular sciences · 2023Article
- Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging.Structure (London, England : 1993) · 2022Article
- Human γS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation.The journal of physical chemistry. B · 2022Article
- Inherited cataracts: Genetic mechanisms and pathways new and old.Experimental eye research · 2021Review
- Adenosine triphosphate energy-independently controls protein homeostasis with unique structure and diverse mechanisms.Protein science : a publication of the Protein Society · 2021Review
- A simple vapor-diffusion method enables protein crystallization inside the HARE serial crystallography chip.Acta crystallographica. Section D, Structural biology · 2021Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Mechanisms of Deamidation of Asparagine Residues and Effects of Main-Chain Conformation on Activation Energy.International journal of molecular sciences · 2020Article
- Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation.Protein science : a publication of the Protein Society · 2020Article
- The multifaceted nature of αB-crystallin.Cell stress & chaperones · 2020Review
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.Biochimica et biophysica acta. General subjects · 2020Article
- Altered Protein Dynamics and Increased Aggregation of Human γS-Crystallin Due to Cataract-Associated Deamidations.Biochemistry · 2019Article
- Biology of Inherited Cataracts and Opportunities for Treatment.Annual review of vision science · 2019Review
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7 authors.
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Abstract
Transparency in the eye lens is maintained via specific, functional interactions among the structural βγ- and chaperone α-crystallins. Here, we report the structure and α-crystallin binding interface of the G18V variant of human γS-crystallin (γS-G18V), which is linked to hereditary childhood-onset cortical cataract. Comparison of the solution nuclear magnetic resonance structures of wild-type and G18V γS-crystallin, both presented here, reveal that the increased aggregation propensity of γS-G18V results from neither global misfolding nor the solvent exposure of a hydrophobic residue but instead involves backbone rearrangement within the N-terminal domain. αB-crystallin binds more strongly to the variant, via a well-defined interaction surface observed via chemical shift differences. In the context of the αB-crystallin structure and the finding that it forms heterogeneous multimers, our structural studies suggest a potential mechanism for cataract formation via the depletion of the finite αB-crystallin population of the lens.
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