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Article

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

Biochimica et biophysica acta. General subjects - 1 Mar 2020

Sprague-Piercy Marc A, Wong Eric, Roskamp Kyle W, Fakhoury Joseph N, Freites J Alfredo, Tobias Douglas J, Martin Rachel W

Abstract excerpt

BACKGROUND: The eye lens crystallins are highly soluble proteins that are required to last the lifespan of an organism due to low protein turnover in the lens. Crystallin aggregation leads to formation of light-scattering aggregates known as cataract. The G18V mutation of human γS-crystallin (γS-G18V), which is associated with childhood-onset cataract, causes structural changes throughout the N-terminal domain...

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Share to alpha-Crystallin B Chain
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Hydrophobic and Hydrophilic Interactions

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Source

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Identifiers

PMID: 31812542
DOI: 10.1016/j.bbagen.2019.129502
PMCID: PMC7434982

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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