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Article

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

PloS one - 1 Jan 2013

Vendra Venkata Pulla Rao, Agarwal Garima, Chandani Sushil, Talla Venu, Srinivasan Narayanaswamy, Balasubramanian Dorairajan

Abstract excerpt

BACKGROUND: We highlight an unrecognized physiological role for the Greek key motif, an evolutionarily conserved super-secondary structural topology of the βγ-crystallins. These proteins constitute the bulk of the human eye lens, packed at very high concentrations in a compact, globular, short-range order, generating transparency. Congenital cataract (affecting 400,000 newborns yearly worldwide), associated with...

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Identifiers

PMID: 23936409
DOI: 10.1371/journal.pone.0070336
PMCID: PMC3735602

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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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Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency.PMID 23936409Read ↗

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Gamma crystallins of the human eye lens.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 ↗

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

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

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

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

Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strandsSemantic 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-associated New Mutants S175G/H181Q of βB2-Crystallin and P24S/S31G of γD-Crystallin are Involved in Protein aggregation by Structural ChangesSemantic proximity Read ↗

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