ArticleBiochemistry2009
The structure of the cataract-causing P23T mutant of human gammaD-crystallin exhibits distinctive local conformational and dynamic changes.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 62 citations in OpenAlex.
- A missense mutation in CRYGD linked with autosomal dominant congenital cataract of aculeiform type.Molecular and cellular biochemistry · 2012Trial
- Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain.Journal of the American Chemical Society · 2022Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- A mutatedInternational journal of ophthalmology · 2021Article
- 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
- Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.Biochimica et biophysica acta. General subjects · 2020Article
- Temperature-Dependent Interactions Explain Normal and Inverted Solubility in a γD-Crystallin Mutant.Biophysical journal · 2019Article
- Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Nature communications · 2017Article
- Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.Protein science : a publication of the Protein Society · 2016Article
- Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein.The Journal of biological chemistry · 2016Article
- Novel mutations in CRYGD are associated with congenital cataracts in Chinese families.Scientific reports · 2016Article
- Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutant.The Journal of biological chemistry · 2015Article
- Exome sequencing identifies novel and recurrent mutations in GJA8 and CRYGD associated with inherited cataract.Human genomics · 2014Article
- Solution NMR structures of Pyrenophora tritici-repentis ToxB and its inactive homolog reveal potential determinants of toxin activity.The Journal of biological chemistry · 2014Article
- Article
- Structure and dynamics of the fish eye lens protein, γM7-crystallin.Biochemistry · 2013Article
- Evolution of crystallins for a role in the vertebrate eye lens.Protein science : a publication of the Protein Society · 2013Review
- The human W42R γD-crystallin mutant structure provides a link between congenital and age-related cataracts.The Journal of biological chemistry · 2013Article
- Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency.PloS one · 2013Article
- Protein misfolding and aggregation in cataract disease and prospects for prevention.Trends in molecular medicine · 2012Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Crystallins are major proteins of the eye lens and essential for lens transparency. Mutations and aging of crystallins cause cataracts, the predominant cause of blindness in the world. In human gammaD-crystallin, the P23T mutant is associated with congenital cataracts. Until now, no atomic structural information has been available for this variant. Biophysical analyses of this mutant protein have revealed dramatically reduced solubility compared to that of the wild-type protein due to self-association into higher-molecular weight clusters and aggregates that retain a nativelike conformation within the monomers [Pande, A., et al. (2005) Biochemistry 44, 2491-2500]. To elucidate the structure and local conformation around the mutation site, we have determined the solution structure and characterized the protein's dynamic behavior by NMR. Although the global structure is very similar to the X-ray structure of wild-type gammaD-crystallin, pivotal local conformational and dynamic differences are caused by the threonine substitution. In particular, in the P23T mutant, the imidazole ring of His22 switches from the predominant Nepsilon2 tautomer in the wild-type protein to the Ndelta1 tautomer, and an altered motional behavior of the associated region in the protein is observed. The data support structural changes that may initiate aggregation or polymerization by the mutant protein.
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