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Article

Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.

Structure (London, England : 1993) - 3 Dec 2013

Kingsley Carolyn N, Brubaker William D, Markovic Stefan, Diehl Anne, Brindley Amanda J, Oschkinat Hartmut, Martin Rachel W

Abstract excerpt

Transparency in the eye lens is maintained via specific, functional interactions among the structural βγ- and chaperone α-crystallins. Here, we report the structure and α-crystallin binding interface of the G18V variant of human γS-crystallin (γS-G18V), which is linked to hereditary childhood-onset cortical cataract. Comparison of the solution nuclear magnetic resonance structures of wild-type and G18V...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 24183572
DOI: 10.1016/j.str.2013.09.017
PMCID: PMC3940334

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.PMID 24183572Read ↗

Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.Semantic proximity Read ↗

Increased hydrophobic surface exposure in the cataract-related G18V variant of human γS-crystallin.Semantic proximity Read ↗

¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.Semantic proximity Read ↗

The cataract-causing mutation G75V promotes γS-crystallin aggregation by modifying and destabilizing the native structure.Semantic proximity Read ↗

Cataract-associated deamidations on the surface of γS-crystallin increase protein unfolding and flexibility at distant regionsSemantic proximity Read ↗

Structural and biochemical characterization of the childhood cataract-associated R76S mutant of human γD-crystallin.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 ↗

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

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

Human Crystallin Variation and Cataract.Semantic proximity Read ↗

The 18th amino acid glycine plays an essential role in maintaining the structural stabilities of γS-crystallin linking with congenital cataract.Semantic proximity Read ↗

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

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