ArticleBiochemistry2013
Structure and dynamics of the fish eye lens protein, γM7-crystallin.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Zebrafish as a model for crystallin-associated congenital cataracts in humans.Frontiers in cell and developmental biology · 2025Review
- Review
- Whole genome assembly of the armored loricariid catfish Ancistrus triradiatus highlights herbivory signatures.Molecular genetics and genomics : MGG · 2022Article
- Eyes and ears: A comparative approach linking the chemical composition of cod otoliths and eye lenses.Journal of fish biology · 2022Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Ultrafast Dynamics of Water-Protein Coupled Motions around the Surface of Eye Crystallin.Journal of the American Chemical Society · 2020Article
- Molecular analysis of population andHeliyon · 2020Article
- γ-Crystallins of the chicken lens: remnants of an ancient vertebrate gene family in birds.The FEBS journal · 2016Article
- γS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.The journal of physical chemistry. B · 2014Article
- The βγ-crystallins: native state stability and pathways to aggregation.Progress in biophysics and molecular biology · 2014Review
- Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.Progress in biophysics and molecular biology · 2014Review
- Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins.Protein science : a publication of the Protein Society · 2014Article
- Unexpected headless and tailless fish in the stomach content of shortfin mako Isurus oxyrinchus.PloS one · 2014Article
- Solution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.Protein science : a publication of the Protein Society · 2014Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The vertebrate eye lens contains high concentrations of crystallins. The dense lenses of fish are particularly abundant in a class called γM-crystallin whose members are characterized by an unusually high methionine content and partial loss of the four tryptophan residues conserved in all γ-crystallins from mammals which are proposed to contribute to protection from UV-damage. Here, we present the structure and dynamics of γM7-crystallin from zebrafish (Danio rerio). The solution structure shares the typical two-domain, four-Greek-key motif arrangement of other γ-crystallins, with the major difference noted in the final loop of the N-terminal domain, spanning residues 65-72. This is likely due to the absence of the conserved tryptophans. Many of the methionine residues are exposed on the surface but are mostly well-ordered and frequently have contacts with aromatic side chains. This may contribute to the specialized surface properties of these proteins that exist under high molecular crowding in the fish lens. NMR relaxation data show increased backbone conformational motions in the loop regions of γM7 compared to those of mouse γS-crystallin and show that fast internal motion of the interdomain linker in γ-crystallins correlates with linker length. Unfolding studies monitored by tryptophan fluorescence confirm results from mutant mouse γS-crystallin and show that unfolding of a βγ-crystallin domain likely starts from unfolding of the variable loop containing the more fluorescently quenched tryptophan residue, resulting in a native-like unfolding intermediate.
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