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Article

Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.

Nature communications - 5 May 2017

Boatz Jennifer C, Whitley Matthew J, Li Mingyue, Gronenborn Angela M, van der Wel Patrick C A

Abstract excerpt

Cataracts cause vision loss through the large-scale aggregation of eye lens proteins as a result of ageing or congenital mutations. The development of new treatments is hindered by uncertainty about the nature of the aggregates and their mechanism of formation. We describe the structure and morphology of aggregates formed by the P23T human γD-crystallin mutant associated with congenital cataracts. At...

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Identifiers

PMID: 28474685
DOI: 10.1038/ncomms15137
PMCID: PMC5424181

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.PMID 28474685Read ↗

Crystal structure of the cataract-causing P23T γD-crystallin mutant.Semantic proximity Read ↗

An internal disulfide locks a misfolded aggregation-prone intermediate in cataract-linked mutants of human γD-crystallinSemantic proximity Read ↗

Congenital Cataract-Causing Mutation G129C in γC-Crystallin Promotes the Accumulation of Two Distinct Unfolding Intermediates That Form Highly Toxic Aggregates.Semantic proximity Read ↗

Cataract-causing mutations S78F and S78P of γD-crystallin decrease protein conformational stability and drive aggregation.Semantic proximity Read ↗

Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallinSemantic proximity Read ↗

Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency.Semantic proximity Read ↗

Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.Semantic proximity Read ↗

NMR study of the cataract-linked P23T mutant of human gammaD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility.Semantic proximity Read ↗

Protein Aggregation and Cataract: Role of Age-Related Modifications and Mutations in α-Crystallins.Semantic proximity Read ↗

Cataract-prone variants of γD-crystallin populate a conformation with a partially unfolded N-terminal domain under native conditionsSemantic proximity Read ↗

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Altered aggregation properties of mutant gamma-crystallins cause inherited cataract.Semantic proximity Read ↗

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