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Article

The Y46D Mutation Destabilizes Dense Packing of the Second Greek Key Pair of Human γC-Crystallin Causing Congenital Nuclear Cataracts.

Biochemistry - 20 Jun 2023

Vendra Venkata Pulla Rao, Ostrowski Christian, Clark Rebecca, Dyba Marzena, Tarasov Sergey G, Hejtmancik J Fielding

Abstract excerpt

The γ-crystallins are highly expressed structural lens proteins comprising four Greek key motifs arranged in two domains. Their globular structure and short-range spatial ordering are essential for lens transparency. Aromatic residues play a vital role in stabilizing Greek key folds by forming Greek key or non-Greek key pairs or tyrosine corners. We investigated the effects of the cataractogenic Y46D mutation in...

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Identifiers

PMID: 37184593
DOI: 10.1021/acs.biochem.2c00628
PMCID: PMC10758276

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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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Research trail→

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The Y46D Mutation Destabilizes Dense Packing of the Second Greek Key Pair of Human γC-Crystallin Causing Congenital Nuclear Cataracts.PMID 37184593Read ↗

Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract.Semantic proximity Read ↗

The importance of the fourth Greek key motif of human γD-crystallin in maintaining lens transparency-the tale told by the tail.Semantic proximity Read ↗

Truncation mutations of CRYGD gene in congenital cataracts cause protein aggregation by disrupting the structural stability of γD-crystallin.Semantic proximity Read ↗

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

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

S209W mutation enhance π-π interactions in the fourth Greek-key of βA3/A1-crystallin linking with aggregation formation and stress susceptibility.Semantic proximity Read ↗

Cataract-causing mutations L45P and Y46D impair the thermal stability of γC-crystallin.Semantic proximity Read ↗

The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly.Semantic proximity Read ↗

Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strandsSemantic 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 ↗

The mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataract.Semantic proximity Read ↗

βB2 W151R mutant is prone to degradation, aggregation and exposes the hydrophobic side chains in the fourth Greek Key motif.Semantic proximity Read ↗

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